|
Name |
Accession |
Description |
Interval |
E-value |
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-606 |
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: 884.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 2 CGIFGYLGEKNAVPLVLEGLSKLEYRGYDSAGIATLVEGRLFVEKAVGPVSQLCSAVS-SDIHSQAAIGHTRWATHGEPS 80
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKLGeKPLPGGVGIGHTRWATHGKPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 81 RFNAHPHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKETRDLIQSFSWTLKRLQGSFACA 160
Cdd:TIGR01135 81 DENAHPHTDEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 161 LMHQDHPEVLLCAAHESPLILGLGEDEVFISSDIHAFLKYSGCTQTLASGELAVLRIGkSIETYNFELARIQKEVRCIDH 240
Cdd:TIGR01135 161 VLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKD-GVEIYNFEGAPVQREVRVIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 241 TEDSLDKKGFDYYMLKELYEQPEVFERILHLTCEENG-FTESFLKGFSLDEIQSLHIVACGSSYHAGYLAKYVIESIASI 319
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGgVFEELGAEELLKNIDRIQIVACGTSYHAGLVAKYLIERLAGI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 320 PVYVETASEFRYRQPYIAEHSLAILISQSGETADTLAALNEFRKLsKARVLGICNVRESALASRVDHCLFIEAGLEVGVA 399
Cdd:TIGR01135 320 PVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKEL-GAKTLGICNVPGSTLVREADHTLYTRAGPEIGVA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 400 STKAFTAQLLLLILLGLRLANHRQVIAQEDLAQAIQGLKDLPNLTR--LFLDSSIHDWRCRQIEETSFIFLGRRFMYPIC 477
Cdd:TIGR01135 399 STKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVEqvLLADESIAELAERYADKRNFLFLGRGLGYPIA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 478 MEAALKLKEIAYVEANAYPAGEMKHGPIALIREGTPVIVYCGDRSVYTKTIGAIMEVKARKAYVIALAPESNRDIAAVSD 557
Cdd:TIGR01135 479 LEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVAD 558
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 15605551 558 EQIYIPDSHDLAAPILFTIAGQIMAYTMALQRGTEVDRPRNLAKSVTVE 606
Cdd:TIGR01135 559 DVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-606 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 839.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 1 MCGIFGYLGEKNAVPLVLEGLSKLEYRGYDSAGIATLVEGRLFVEKAVGPVSQLCSAV-SSDIHSQAAIGHTRWATHGEP 79
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLeEEPLPGTTGIGHTRWATHGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 80 SRFNAHPHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKETRDLIQSFSWTLKRLQGSFAC 159
Cdd:PRK00331 81 TERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 160 ALMHQDHPEVLLCAAHESPLILGLGEDEVFISSDIHAFLKYSGCTQTLASGELAVLRIGkSIETYNFELARIQKEVRCID 239
Cdd:PRK00331 161 AVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRD-GVEIFDFDGNPVEREVYTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 240 HTEDSLDKKGFDYYMLKELYEQPEVFERIL--HLTCEENGftesFLKGFSLDEIQSLHIVACGSSYHAGYLAKYVIESIA 317
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLegRLDELGEG----ELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 318 SIPVYVETASEFRYRQPYIAEHSLAILISQSGETADTLAALNEFRKLsKARVLGICNVRESALASRVDHCLFIEAGLEVG 397
Cdd:PRK00331 316 GIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKEL-GAKTLAICNVPGSTIARESDAVLYTHAGPEIG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 398 VASTKAFTAQLLLLILLGLRLANHRQVIAQEDLAQAIQGLKDLPNLTRLFLDS--SIHDWRCRQIEETSFIFLGRRFMYP 475
Cdd:PRK00331 395 VASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLkeQIEELAEDFADARNALFLGRGVDYP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 476 ICMEAALKLKEIAYVEANAYPAGEMKHGPIALIREGTPVIVYCGDRSVYTKTIGAIMEVKARKAYVIALAPESNrDIAAV 555
Cdd:PRK00331 475 VALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGD-EVAEE 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 15605551 556 SDEQIYIPDSHDLAAPILFTIAGQIMAYTMALQRGTEVDRPRNLAKSVTVE 606
Cdd:PRK00331 554 ADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-606 |
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: 826.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 1 MCGIFGYLGEKNAVPLVLEGLSKLEYRGYDSAGIATLVEGRLFVEKAVGPVSQLCSAV-SSDIHSQAAIGHTRWATHGEP 79
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLaEEPLSGTIGIGHTRWATHGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 80 SRFNAHPHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKETRDLIQSFSWTLKRLQGSFAC 159
Cdd:COG0449 81 SDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 160 ALMHQDHPEVLLCAAHESPLILGLGEDEVFISSDIHAFLKYsgcTQT---LASGELAVLRiGKSIETYNFELARIQKEVR 236
Cdd:COG0449 161 AVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPY---TRRviyLEDGEIAVLT-RDGVEIYDLDGEPVEREVK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 237 CIDHTEDSLDKKGFDYYMLKELYEQPEVFERIL-HLTCEENGFTESFLK--GFSLDEIQSLHIVACGSSYHAGYLAKYVI 313
Cdd:COG0449 237 TVDWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLrGRLDEDGRVVLDELNlaAEDLRNIDRIYIVACGTSYHAGLVGKYLI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 314 ESIASIPVYVETASEFRYRQPYIAEHSLAILISQSGETADTLAALNEFRKLsKARVLGICNVRESALASRVDHCLFIEAG 393
Cdd:COG0449 317 EELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEK-GAKVLAICNVVGSTIARESDAVLYTHAG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 394 LEVGVASTKAFTAQLLLLILLGLRLANHRQVIAQEDLAQAIQGLKDLPNLTR--LFLDSSIHDWRCRQIEETSFIFLGRR 471
Cdd:COG0449 396 PEIGVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIEevLDLEEQIEELAEKYADARNALFLGRG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 472 FMYPICMEAALKLKEIAYVEANAYPAGEMKHGPIALIREGTPVIVYCGDRSVYTKTIGAIMEVKARKAYVIALAPESNRD 551
Cdd:COG0449 476 INYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEE 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 15605551 552 IAAVSDEQIYIPDSHDLAAPILFTIAGQIMAYTMALQRGTEVDRPRNLAKSVTVE 606
Cdd:COG0449 556 VEELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-605 |
1.36e-151 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 451.01 E-value: 1.36e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 1 MCGIFGYLGEKNAVPLVLEGLSKLEYRGYDSAGIATLVEGRLFVekavgpVSQLCS--------------AVSSDIHSQA 66
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELK------TTKYASdgttsdsieilkekLLDSHKNSTI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 67 AIGHTRWATHGEPSRFNAHPHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKETRDLIQSF 146
Cdd:PTZ00295 98 GIAHTRWATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 147 SWTLKRLQGSFACALMHQDHPEVLLCAAHESPLILGLGEDEVFISSDIHAFLKYSGCTQTLASGELAVLRIGKSIETYNf 226
Cdd:PTZ00295 178 KSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYT- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 227 elariQKEVRCIDHTEDSLDKKGFDYYMLKELYEQPEVFERILHLTCEENGFTESF-LKGF-----SLDEIQSLHIVACG 300
Cdd:PTZ00295 257 -----QRRVEKIPEEVIEKSPEPYPHWTLKEIFEQPIALSRALNNGGRLSGYNNRVkLGGLdqyleELLNIKNLILVGCG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 301 SSYHAGYLAKYVIESIASI-PVYVETASEF-RYRQPYiaEHSLAILISQSGETADTLAALNEFRKLSkARVLGICNVRES 378
Cdd:PTZ00295 332 TSYYAALFAASIMQKLKCFnTVQVIDASELtLYRLPD--EDAGVIFISQSGETLDVVRALNLADELN-LPKISVVNTVGS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 379 ALASRVDHCLFIEAGLEVGVASTKAFTAQLLLLILLGLRLANHRQVIAQED-LAQAIQGLKDLPNLTRLFLDSSihDWRC 457
Cdd:PTZ00295 409 LIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNYkCSSLINSLHRLPTYIGMTLKSC--EEQC 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 458 RQIEE-----TSFIFLGRRFMYPICMEAALKLKEIAYVEANAYPAGEMKHGPIALI--REGTPVIVYCGDRSVYTKTIGA 530
Cdd:PTZ00295 487 KRIAEklknaKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIdkEKNTPVILIILDDEHKELMINA 566
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15605551 531 IMEVKARKAYVIALA--PESNRDIAavsDEQIYIPdSHDLAAPILFTIAGQIMAYTMALQRGTEVDRPRNLAKSVTV 605
Cdd:PTZ00295 567 AEQVKARGAYIIVITddEDLVKDFA---DEIILIP-SNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-606 |
4.00e-122 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 376.40 E-value: 4.00e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 1 MCGIFGYLG------EKNAVPLVLEGLSKLEYRGYDSAGIATLVEGRL-----FVEKAVGPVSQLCSAVSSDI------- 62
Cdd:PLN02981 1 MCGIFAYLNynvpreRRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLessspLVFREEGKIESLVRSVYEEVaetdlnl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 63 ----HSQAAIGHTRWATHGEPSRFNAHPHV-DMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQL----FA 133
Cdd:PLN02981 81 dlvfENHAGIAHTRWATHGPPAPRNSHPQSsGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLakfvFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 134 RRYKETRDLiqSFSW----TLKRLQGSFACALMHQDHPEVLLCAAHESPLILGLGED----------------------- 186
Cdd:PLN02981 161 KLNEEEGDV--TFSQvvmeVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKELpeeknssavftsegfltknrdkp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 187 -EVFISSDIHAFLKYSGCTQTLASGELAVLRIGkSIETYNFELAR------------IQKEVRCIDHTEDSLDKKGFDYY 253
Cdd:PLN02981 239 kEFFLASDASAVVEHTKRVLVIEDNEVVHLKDG-GVGIYKFENEKgrgggglsrpasVERALSTLEMEVEQIMKGNYDHY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 254 MLKELYEQPEVFERIL--HLTCEENGFTESFLKGFSLDEIQSLH------IVACGSSYHAGYLAKYVIESIASIPVYVET 325
Cdd:PLN02981 318 MQKEIHEQPESLTTTMrgRLIRGGSGKAKRVLLGGLKDHLKTIRrsrrivFIGCGTSYNAALAARPILEELSGVPVTMEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 326 ASEFRYRQPYIAEHSLAILISQSGETADTLAALnEFRKLSKARVLGICNVRESALaSRVDHC-LFIEAGLEVGVASTKAF 404
Cdd:PLN02981 398 ASDLLDRQGPIYREDTAVFVSQSGETADTLRAL-EYAKENGALCVGITNTVGSAI-SRGTHCgVHINAGAEIGVASTKAY 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 405 TAQLLLLILLGLRLANHrQVIAQEDLAQAIQGLKDLPNLTR--LFLDSSIHDWRCRQIEETSFIFLGRRFMYPICMEAAL 482
Cdd:PLN02981 476 TSQIVAMTMLALALGED-SISSRSRREAIIDGLFDLPNKVRevLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGAL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 483 KLKEIAYVEANAYPAGEMKHGPIALIREGTPVIVYCGDRSVYTKTIGAIMEVKARKAYVIALAPESNRDIAAVSDEQ--I 560
Cdd:PLN02981 555 KVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDASSVCPSGGCrvI 634
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 15605551 561 YIPDSHDLAAPILFTIAGQIMAYTMALQRGTEVDRPRNLAKSVTVE 606
Cdd:PLN02981 635 EVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-606 |
6.77e-119 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 367.67 E-value: 6.77e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 1 MCGIFGYLGE------KNAVPLVLEGLSKLEYRGYDSAGI---------------ATLVEGRLFVEKAVGPVSQLCSAVS 59
Cdd:PTZ00394 1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLaidanigsekedgtaASAPTPRPCVVRSVGNISQLREKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 60 SD------------IHSQAAIGHTRWATHGEPSRFNAHPHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEV 127
Cdd:PTZ00394 81 SEavaatlppmdatTSHHVGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 128 IVQLfaRRYKETRDLIQSFSWTLKR----LQGSFACALMHQDHPEVLLCAAHESPLILGL-------------------- 183
Cdd:PTZ00394 161 ISVL--SEYLYTRKGIHNFADLALEvsrmVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydltdl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 184 -GEDEVFISSDIHAFLKYSGCTQTLASGELAVLRIGkSIETYNFE---LARIQKEVRCIDHTEDSLDKKGFDYYMLKELY 259
Cdd:PTZ00394 239 sGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDG-ALRFYNAAerqRSIVKREVQHLDAKPEGLSKGNYPHFMLKEIY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 260 EQPEVFERILHLTCEENGFTESFlKGFSLDEIQSL------HIVACGSSYHAGYLAKYVIESIASIPVYVETASEFRYRQ 333
Cdd:PTZ00394 318 EQPESVISSMHGRIDFSSGTVQL-SGFTQQSIRAIltsrriLFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 334 PYIAEHSLAILISQSGETADTLAALnEFRKLSKARVLGICNVRESALASRVDHCLFIEAGLEVGVASTKAFTAQLLLLIL 413
Cdd:PTZ00394 397 PRIQRDDVCFFVSQSGETADTLMAL-QLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 414 LGLRLANHRQVIaQEDLAQAIQGLKDLPNLTR---LFLDSSIHDWRCRQIEETSFIFLGRRFMYPICMEAALKLKEIAYV 490
Cdd:PTZ00394 476 VALLLSSDSVRL-QERRNEIIRGLAELPAAISeclKITHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYV 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 491 EANAYPAGEMKHGPIALIREGTPVIVYCGDRSVYTKTIGAIMEVKARKAYVIALAPESNRDIAAVSDEQIYIPDSHDLAA 570
Cdd:PTZ00394 555 HTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTVDCLQ 634
|
650 660 670
....*....|....*....|....*....|....*.
gi 15605551 571 PILFTIAGQIMAYTMALQRGTEVDRPRNLAKSVTVE 606
Cdd:PTZ00394 635 CVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-215 |
5.39e-105 |
|
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: 315.93 E-value: 5.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 2 CGIFGYLGEKNAVPLVLEGLSKLEYRGYDSAGIATLVEGRLFVEKAVGPVSQLCSAVSSD-IHSQAAIGHTRWATHGEPS 80
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKpLSGHVGIGHTRWATHGEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 81 RFNAHPHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKETRDLIQSFSWTLKRLQGSFACA 160
Cdd:cd00714 81 DVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYALA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15605551 161 LMHQDHPEVLLCAAHESPLILGLGEDEVFISSDIHAFLKYsgcTQT---LASGELAVL 215
Cdd:cd00714 161 VISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEH---TRRviyLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
255-606 |
5.94e-70 |
|
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: 229.40 E-value: 5.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 255 LKELYEQPEVFERILHLTCEEngfTESFLKGFSLDEIQSLHIVACGSSYHAGYLAKYVIESIASIPVYVETASEF-RYRQ 333
Cdd:COG2222 1 AREIAQQPEAWRRALAALAAA---IAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvVYPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 334 PYIAEHSLAILISQSGETADTLAALNEFRKLsKARVLGICNVRESALASRVDHCLFIEAGLEVGVASTKAFTAQLLLlil 413
Cdd:COG2222 78 YLKLEGTLVVAISRSGNSPEVVAALELAKAR-GARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLA--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 414 lglrlanHRQVIAQEDLAQAIQG-LKDLPNLTRLFLDSSIHDWRCRQIEE-TSFIFLGRRFMYPICMEAALKLKEIAYVE 491
Cdd:COG2222 154 -------LLALLAAWGGDDALLAaLDALPAALEAALAADWPAAALAALADaERVVFLGRGPLYGLAREAALKLKELSAGH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 492 ANAYPAGEMKHGPIALIREGTPVIVYCGDRSVYTKTIGAIMEVKARKAYVIALAPESNRDIAAVSdeqiyIPDSHDLAAP 571
Cdd:COG2222 227 AEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPA-----IPDLHDALDP 301
|
330 340 350
....*....|....*....|....*....|....*
gi 15605551 572 ILFTIAGQIMAYTMALQRGTEVDRPRNLAKSVTVE 606
Cdd:COG2222 302 LLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-213 |
1.14e-57 |
|
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: 193.05 E-value: 1.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 2 CGIFGYLGEKNAVPLVLE----GLSKLEYRGYDSAGIATLVEGRLFVEKAVGPVSQLCSAV-SSDIHSQAAIGHTRWATH 76
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLlDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 77 GEPSRFNAHPHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKEtRDLIQSFSWTLKRLQGS 156
Cdd:cd00352 81 GLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGRE-GGLFEAVEDALKRLDGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15605551 157 FACALMHqDHPEVLLCAAH---ESPLILGLGED-EVFISSDIHAFLKYSGCT-QTLASGELA 213
Cdd:cd00352 160 FAFALWD-GKPDRLFAARDrfgIRPLYYGITKDgGLVFASEPKALLALPFKGvRRLPPGELL 220
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
461-604 |
9.25e-54 |
|
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: 180.15 E-value: 9.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 461 EETSFIFLGRRFMYPICMEAALKLKEIAYVEANAYPAGEMKHGPIALIREGTPVIVYCGDRSVYTKTIGAIMEVKARKAY 540
Cdd:cd05009 12 EAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESLIKEVKARGAK 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15605551 541 VIALAPESnrDIAAVSDEQIYIPDSHDLAAPILFTIAGQIMAYTMALQRGTEVDRPRNLAKSVT 604
Cdd:cd05009 92 VIVITDDG--DAKDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
294-407 |
3.87e-49 |
|
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: 166.90 E-value: 3.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 294 LHIVACGSSYHAGYLAKYVIESIASIPVYVETASEFRYRQPYIAEHSLAILISQSGETADTLAALNEFRKLsKARVLGIC 373
Cdd:cd05008 2 ILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEK-GAKTVAIT 80
|
90 100 110
....*....|....*....|....*....|....
gi 15605551 374 NVRESALASRVDHCLFIEAGLEVGVASTKAFTAQ 407
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQ 114
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-192 |
8.09e-40 |
|
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: 146.07 E-value: 8.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 2 CGIFGYLGEKNAVPLVLEGLSKLEYRGYDSAGIATLVEGRLFVEKAVGPVSQLCSA-VSSDIHSQAAIGHTRWATHGEPS 80
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEeKLRRLPGNIAIGHVRYSTAGSSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 81 RFNAHPHVdmdASC-----ALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFArRYKETRDLIQSFSWTLKRLQG 155
Cdd:cd00715 81 LENAQPFV---VNSplggiALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIA-RSLAKDDLFEAIIDALERVKG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15605551 156 SFACALMHQDHpevlLCAAHES----PLILG-LGEDEVFISS 192
Cdd:cd00715 157 AYSLVIMTADG----LIAVRDPhgirPLVLGkLEGDGYVVAS 194
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-165 |
1.10e-39 |
|
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: 151.33 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 1 MCGIFGYLGEKNAVPLVLEGLSKLEYRGYDSAGIATLVEGRLFVEKAVGPVSQ-LCSAVSSDIHSQAAIGHTRWATHGEP 79
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDvFDEEDLERLKGNIAIGHVRYSTTGSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 80 SRFNAHPHVdmdASC-----ALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFArRYKETRDLIQSFSWTLKRLQ 154
Cdd:COG0034 87 SLENAQPFY---VNSpfgsiALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIA-RELTKEDLEEAIKEALRRVK 162
|
170
....*....|.
gi 15605551 155 GSFACALMHQD 165
Cdd:COG0034 163 GAYSLVILTGD 173
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-197 |
8.50e-34 |
|
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: 133.98 E-value: 8.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 2 CGIFGYLGEKNAVPLVL-EGLSKLEYRGYDSAGIATLVEGRLFVEKAVGPVSQLCSAVS-SDIHSQAAIGHTRWATHGEP 79
Cdd:TIGR01134 1 CGVVGIYGQEEVAASLTyYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHlQRLKGNVGIGHVRYSTAGSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 80 SRFNAHPHV--DMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKETRDLIQSFSWTLKRLQGSF 157
Cdd:TIGR01134 81 GLENAQPFVvnSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRGAY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15605551 158 ACALMHQDHpevlLCAAHES----PLILGLGEDEVFISSDIHAF 197
Cdd:TIGR01134 161 ALVLMTEDG----LVAVRDPhgirPLVLGRRGDGYVVASESCAL 200
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-197 |
5.44e-26 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 111.28 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 2 CGIFGYLGEKN--AVPLVLEGLSKLEYRGYDSAGIATLVEGRLFVEKAVGPVSQLCSAVSSD-IHSQAAIGHTRWATHGE 78
Cdd:PRK05793 15 CGVFGVFSKNNidVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKgLKGNSAIGHVRYSTTGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 79 PSRFNAHPHVD--MDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKetRDLIQSFSWTLKRLQGS 156
Cdd:PRK05793 95 SDLDNAQPLVAnyKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAK--KGLEKALVDAIQAIKGS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15605551 157 FACALMHQDHpevlLCAAHE----SPLILGLGEDEVFISSDIHAF 197
Cdd:PRK05793 173 YALVILTEDK----LIGVRDphgiRPLCLGKLGDDYILSSESCAL 213
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-197 |
1.15e-24 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 107.46 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 1 MCGIFGYLGEKNAVPLVLEGLSKLEYRGYDSAGIATLVEGRLFVEKAVGPVSQLCSAVSSD-IHSQAAIGHTRWATHGEP 79
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDqLPGDIAIGHVRYSTAGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 80 SRFNAHPHVdmdASC-----ALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKetRDLIQSFSWTLKRLQ 154
Cdd:PLN02440 81 SLKNVQPFV---ANYrfgsiGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKA--RPFFSRIVDACEKLK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15605551 155 GSFACALMHQDhpevLLCAAHES----PLILGL-GEDEVFISSDIHAF 197
Cdd:PLN02440 156 GAYSMVFLTED----KLVAVRDPhgfrPLVMGRrSNGAVVFASETCAL 199
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
296-407 |
1.26e-23 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 96.60 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 296 IVACGSSYHAGYLAKYVIESIASIPVYVETASEFRYRQ-PYIAEHSLAILISQSGETADTLAALNEFRKLsKARVLGICN 374
Cdd:pfam01380 10 VIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVlALVDEDDLVIAISYSGETKDLLAAAELAKAR-GAKIIAITD 88
|
90 100 110
....*....|....*....|....*....|...
gi 15605551 375 VRESALASRVDHCLFIEAGLEVGVASTKAFTAQ 407
Cdd:pfam01380 89 SPGSPLAREADHVLYINAGPETGVASTKSITAQ 121
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-215 |
1.33e-19 |
|
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: 87.61 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 2 CGIFGYL---GEKNAVPLVLEGLSKLEYRGYDSAGIAtlvegrlfvekavgpvsqlcsavssdIHSQAAIGHTRWATHGE 78
Cdd:cd00712 1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGIW--------------------------IDEGVALGHRRLSIIDL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 79 psRFNAHPHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFaRRYKETrdliqsfswTLKRLQGSFA 158
Cdd:cd00712 55 --SGGAQPMVSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLY-EEWGED---------CLERLNGMFA 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 159 CALmHQDHPEVLLCA---AHESPLILGLGEDEVFISSDIHAFLKYSGCTQTLASGELAVL 215
Cdd:cd00712 123 FAL-WDKRKRRLFLArdrFGIKPLYYGRDGGGLAFASELKALLALPGVPRELDEAALAEY 181
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
62-161 |
4.21e-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: 83.51 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 62 IHSQAAIGHTRWATHGEPSRFNaHPHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKEtrd 141
Cdd:pfam13522 8 VEGGVALGHVRLAIVDLPDAGN-QPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEWGED--- 83
|
90 100
....*....|....*....|
gi 15605551 142 liqsfswTLKRLQGSFACAL 161
Cdd:pfam13522 84 -------CLERLRGMFAFAI 96
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
91-198 |
4.85e-18 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 80.25 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 91 DASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKETrdliqsfswTLKRLQGSFACALMHQDHPEVL 170
Cdd:pfam13537 21 DGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEWGED---------CVDRLNGMFAFAIWDRRRQRLF 91
|
90 100 110
....*....|....*....|....*....|.
gi 15605551 171 LCAAH--ESPLILGLGEDEVFI-SSDIHAFL 198
Cdd:pfam13537 92 LARDRfgIKPLYYGRDDGGRLLfASELKALL 122
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-196 |
1.04e-17 |
|
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: 83.09 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 2 CGIFGYL---GEKNAVPLVLEGLSKLEYRG-YDSAGIA--TLVEGRLF-------VEKAVGPVSQLCSAVS-SDIHSQAA 67
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFAlyGDPDAFVYssgkdmeVFKGVGYPEDIARRYDlEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 68 IGHTRWATHGEPSRFNAHPHVDMDAscALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKETRDLIQSF- 146
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPFSIGDI--AVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEYYk 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15605551 147 ------------------SWTLKRLQGSFACALMHQDHPEVLLCAAHESPLILGLGEDEVFISSDIHA 196
Cdd:cd01907 159 hiirmpeeerelllalrlTYRLADLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECA 226
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
466-587 |
7.34e-17 |
|
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: 77.34 E-value: 7.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 466 IFLGRRFMYPICMEAALKLKEIAYVEANAYPAGEMKHGPIALIREGTPVIVycGDRSVYTK-TIGAIMEVKARKAYVIAL 544
Cdd:pfam01380 9 FVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIA--ISYSGETKdLLAAAELAKARGAKIIAI 86
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15605551 545 APESNRDIAAVSDEQIYIPDSHDLAAPILFTIAGQIMAYTMAL 587
Cdd:pfam01380 87 TDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALA 129
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-202 |
1.09e-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: 83.35 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 1 MCGIFGYLGEKNAV--PLVLEGLSKLEYRGYDSAGIAtlvegrlfvekavgpvsqlcsavssdIHSQAAIGHTRWATHGE 78
Cdd:COG0367 1 MCGIAGIIDFDGGAdrEVLERMLDALAHRGPDGSGIW--------------------------VDGGVALGHRRLSIIDL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 79 PSRfnAH-PHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFaRRYKETrdliqsfswTLKRLQGSF 157
Cdd:COG0367 55 SEG--GHqPMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAY-EEWGED---------CLERLNGMF 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15605551 158 ACALMHQDHPEVLLCAAH--ESPLILGLGEDEVFISSDIHAFLKYSG 202
Cdd:COG0367 123 AFAIWDRRERRLFLARDRfgIKPLYYAEDGGGLAFASELKALLAHPG 169
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
297-393 |
1.78e-16 |
|
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: 75.69 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 297 VACGSSYHAGYLAKYVIESIASIPVYVETASEFRYRQP-YIAEHSLAILISQSGETADTLAAlNEFRKLSKARVLGICNV 375
Cdd:cd05710 5 VGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPkRLTEKSVVILASHSGNTKETVAA-AKFAKEKGATVIGLTDD 83
|
90
....*....|....*...
gi 15605551 376 RESALASRVDHCLFIEAG 393
Cdd:cd05710 84 EDSPLAKLADYVIVYGFE 101
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-128 |
1.40e-11 |
|
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238889 [Multi-domain] Cd Length: 257 Bit Score: 65.10 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 1 MCGIFGYLGEKN-AVPLVLEGLSKL--------EYRGY---DSAGIA--TLVEGRLFVEKAVGPVSQLCSAVSSD--IHS 64
Cdd:cd01908 1 MCRLLGYSGAPIpLEPLLIRPSHSLlvqsggprEMKGTvhaDGWGIGwyEGKGGRPFRYRSPLPAWSDINLESLArpIKS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15605551 65 QAAIGHTRWATHGEPSRFNAHPHVDMDAscALVHNGIIENFQKLKEELEEQGVVFS-SDTDTEVI 128
Cdd:cd01908 81 PLVLAHVRAATVGPVSLENCHPFTRGRW--LFAHNGQLDGFRLLRRRLLRLLPRLPvGTTDSELA 143
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-161 |
2.57e-11 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 66.47 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 1 MCGIFGYLGEKNAV----PLVLEGLSKLEYRGYDSAGIatlvegrlfvekavgpvsqlcsaVSSDihsQAAIGHTRWA-- 74
Cdd:PRK09431 1 MCGIFGILDIKTDAdelrKKALEMSRLMRHRGPDWSGI-----------------------YASD---NAILGHERLSiv 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 75 --THGEPSRFNAhphvdmDASCALVHNGIIENFQKLKEELEEqGVVFSSDTDTEVIVQLFarryketRDLIQSFswtLKR 152
Cdd:PRK09431 55 dvNGGAQPLYNE------DGTHVLAVNGEIYNHQELRAELGD-KYAFQTGSDCEVILALY-------QEKGPDF---LDD 117
|
....*....
gi 15605551 153 LQGSFACAL 161
Cdd:PRK09431 118 LDGMFAFAL 126
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
2-222 |
2.90e-11 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 63.83 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 2 CGIFGYLGEK--NAVPLVLEGLSKLEYRGYDSA--------GIATLVE-GRLFVEKAVGPV--SQLCSAVSSDIHSQAAI 68
Cdd:COG0121 1 CRLLGYSGNVptDLEFLLLDPEHSLVRQSGATRegphadgwGIGWYEGdGEPRLYRDPLPAwsDPNLRLLARPIKSRLVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 69 GHTRWATHGEPSRFNAHPHVdmDASCALVHNGIIENFQKLKEELEEQGVVFS-----SDTDTEVIVQLFARRYKET-RDL 142
Cdd:COG0121 81 AHVRKATVGPVSLENTHPFR--GGRWLFAHNGQLDGFDRLRRRLAEELPDELyfqpvGTTDSELAFALLLSRLRDGgPDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 143 IQSFSWTLKRLQ------GSFACALMhqDhPEVL--LCAAHESP------LILGLGEDEVFI--SSDihafLKYSGCTQT 206
Cdd:COG0121 159 AEALAEALRELAelarapGRLNLLLS--D-GERLyaTRYTSDDPyptlyyLTRTTPDDRVVVvaSEP----LTDDEGWTE 231
|
250
....*....|....*.
gi 15605551 207 LASGELAVLRIGKSIE 222
Cdd:COG0121 232 VPPGELLVVRDGLEVE 247
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-196 |
4.59e-10 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 62.42 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 1 MCGI---FGYLGEKNAV-PLVLEGLSKLEYRGYDSAGIATLvegrlfvekavgpvsqlcsavSSDIHSQAAIGHTRWATH 76
Cdd:PTZ00077 1 MCGIlaiFNSKGERHELrRKALELSKRLRHRGPDWSGIIVL---------------------ENSPGTYNILAHERLAIV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 77 GEPSrfNAHPHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFaRRYKETRdliqsfswTLKRLQGS 156
Cdd:PTZ00077 60 DLSD--GKQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLY-KEYGPKD--------FWNHLDGM 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15605551 157 FACALMhqDHPEVLLCAAHES----PLILGLGED-EVFISSDIHA 196
Cdd:PTZ00077 129 FATVIY--DMKTNTFFAARDHigiiPLYIGYAKDgSIWFSSELKA 171
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-161 |
1.50e-08 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 57.34 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 4 IFGYLGEKNAV----PLVLEGLSKLEYRGYDSAGIAtlvegrlfvekavgpvsqlcsavssDIHSQAAIGHTRWA----- 74
Cdd:TIGR01536 1 IAGFFDLDDKAveedEAIKRMSDTIAHRGPDASGIE-------------------------YKDGNAILGHRRLAiidls 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 75 THGEPSRFNAHPHVdmdascaLVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFaRRYKETrdliqsfswTLKRLQ 154
Cdd:TIGR01536 56 GGAQPMSNEGKTYV-------IVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLY-EEWGEE---------CVDRLD 118
|
....*..
gi 15605551 155 GSFACAL 161
Cdd:TIGR01536 119 GMFAFAL 125
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
288-392 |
2.17e-08 |
|
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.
Pssm-ID: 240144 [Multi-domain] Cd Length: 139 Bit Score: 53.00 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 288 LDEIQSLHIVACGSSYHAGYLAKYVIESIASIPVYVETASEFRYRQPYIAEHSLAILISQSGETADTLAALNEFRKlSKA 367
Cdd:cd05013 10 LAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKE-RGA 88
|
90 100
....*....|....*....|....*
gi 15605551 368 RVLGICNVRESALASRVDHCLFIEA 392
Cdd:cd05013 89 KVIAITDSANSPLAKLADIVLLVSS 113
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
466-596 |
1.76e-07 |
|
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: 50.70 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 466 IFLGRRFMYPICMEAALKLKEIAyveANAYPA-----GEMKHGPIALIREGTPVIVYCGDRSvYTKT--IGAIMEVKARK 538
Cdd:cd05010 2 VYLGSGPLAGLAREAALKVLELT---AGKVATvydspLGFRHGPKSLVDDDTLVVVFVSNDP-YTRQydLDLLKELRRDG 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15605551 539 --AYVIALAPESNRDIAAVSD----EQIYIPDSHdLAAPilFTIAGQIMAYTMALQRGTEVDRP 596
Cdd:cd05010 78 iaARVIAISPESDAGIEDNSHyylpGSRDLDDVY-LAFP--YILYAQLFALFNSIALGLTPDNP 138
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
296-370 |
3.81e-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: 45.44 E-value: 3.81e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15605551 296 IVACGSSYHAGYLAKYVIESIASIPVYVETASEFRYRQP--YIAEHSLAILISQSGETADTLAALNEFRKLSKARVL 370
Cdd:cd04795 3 VIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLlsLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIA 79
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
290-597 |
6.83e-06 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 48.46 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 290 EIQSLHIVACGSSYHAGYLAKYVIESIASIPVYVETASEFRYRQPYIAEHSLAIL-ISQSGETADTLAALnefrKLSKAr 368
Cdd:PRK11382 43 DIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYRLDDRCAVIgVSDYGKTEEVIKAL----ELGRA- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 369 vlgiCNVRESALASRVDHClfIEAGLEVGVASTKAFTAQLLLLILLGLRLANHRQVIAQEDLAQAIQGLKDLPNLtrlfL 448
Cdd:PRK11382 118 ----CGALTAAFTKRADSP--ITSAAEFSIDYQADCIWEIHLLLCYSVVLEMITRLAPNAEIGKIKNDLKQLPNA----L 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 449 DSSIHDW--RCRQIEETSFIFlgrRFMYPICM---------EAALKLKEIAYVEANAYPAGEMKHGPIALIREGTPVIVY 517
Cdd:PRK11382 188 GHLVRTWeeKGRQLGELASQW---PMIYTVAAgplrplgykEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 518 CGDRSVYTKTIGAIMEVKARKAYVIALapesnrDIAAVSDeqiyipDSHDLAAPILFTIAGQIMAYTMALQRGTEVDRPR 597
Cdd:PRK11382 265 LGNDESRHTTERAINFVKQRTDNVIVI------DYAEISQ------GLHPWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
295-392 |
9.30e-06 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 47.61 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 295 HIVACGSSYH-AGYLA-------KYVIESIASIPVYVETASEfryrqpyIAEHSLAILISQSGETADTLAALNEFRKlSK 366
Cdd:COG1737 138 YIFGVGASAPvAEDLAykllrlgKNVVLLDGDGHLQAESAAL-------LGPGDVVIAISFSGYTRETLEAARLAKE-RG 209
|
90 100
....*....|....*....|....*.
gi 15605551 367 ARVLGICNVRESALASRVDHCLFIEA 392
Cdd:COG1737 210 AKVIAITDSPLSPLAKLADVVLYVPS 235
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
336-407 |
3.97e-05 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 45.93 E-value: 3.97e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15605551 336 IAEHSLAILISQSGETADTLAALNEFRKLsKARVLGICNVRESALASRVDHCLFIEAGLEVGVAST--KAFTAQ 407
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARER-GALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQ 201
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
336-407 |
1.97e-04 |
|
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.
Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 41.37 E-value: 1.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15605551 336 IAEHSLAILISQSGETaDTLAALNEFRKLSKARVLGICNVRESALASRVDHCLFI----EAGLEvGVASTKAFTAQ 407
Cdd:cd05014 45 VTPGDVVIAISNSGET-DELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLpveeEACPL-GLAPTTSTTAM 118
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
254-372 |
1.60e-03 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 41.12 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 254 MLKELYEQPEVFErilhltcEENGFTESFLKGFSLDEIQSLHIVACGSSYHAGYLAKYVIESIASIPVYVetaseFR-YR 332
Cdd:PRK08674 4 MLEEYLNWPEQFE-------EALEIAISLDLEEDLEKIDNIVISGMGGSGIGGDLLRILLFDELKVPVFV-----NRdYT 71
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15605551 333 QP-YIAEHSLAILISQSGETADTLAALNEFRKLsKARVLGI 372
Cdd:PRK08674 72 LPaFVDEKTLVIAVSYSGNTEETLSAVEQALKR-GAKIIAI 111
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
466-545 |
2.05e-03 |
|
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: 37.74 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15605551 466 IFLGRRFMYPICMEAALKLKEIAYVEANAYPAGEMKHGP-IALIREGTPVIVYCGdRSVYTKTIGAIMEVKARKAYVIAL 544
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSY-SGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 15605551 545 A 545
Cdd:cd04795 81 T 81
|
|
| |
