|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-681 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 933.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 1 MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGLDggNDKDWEANACKIqlIKKKGKVKALDEEVHK---QQ 77
Cdd:PLN02981 1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID--NDPSLESSSPLV--FREEGKIESLVRSVYEevaET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 78 DMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVK 157
Cdd:PLN02981 77 DLNLDLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 158 YMYD--NWESQDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEhklstdhipilyrtGKDKKGS 235
Cdd:PLN02981 157 FVFDklNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKEL--------------PEEKNSS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 236 cglSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTARDHPG---------RAV 306
Cdd:PLN02981 223 ---AVFTSEGFLTKNRDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGglsrpasveRAL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 307 QTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDD----YTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGM 382
Cdd:PLN02981 300 STLEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLIRGGsgkaKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAAL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 383 ATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGV 462
Cdd:PLN02981 380 AARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 463 HINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLI 542
Cdd:PLN02981 460 HINAGAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLV 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 543 MGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDK 622
Cdd:PLN02981 540 FGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSK 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54400724 623 EDTETIKNTK--RTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:PLN02981 620 GDASSVCPSGgcRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-681 |
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: 797.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 1 MCGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVG-LDGGndkdweanacKIQLIKKKGKVKALDEEVHKQqdm 79
Cdd:COG0449 1 MCGIVGYI------GKRDAAPILLEGLKRLEYRGYDSAGIAvLDDG----------GLEVRKAVGKLANLEEKLAEE--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 80 dldiEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNeFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYM 159
Cdd:COG0449 62 ----PLSGTIGIGHTRWATHGAPSDENAHPHTSCSGR-IAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 160 YDnwesQDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtGKDkkgscgls 239
Cdd:COG0449 137 LK----GGGDLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL-----------------GEG-------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 240 rvdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTARDhpgRAVQTLQMELQQIMKG 319
Cdd:COG0449 188 ----------------ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVE---REVKTVDWDAEAAEKG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 320 NFSSFMQKEIFEQPESVVNTMRGRVNfDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGMATRQVLEELTELPVMVE 399
Cdd:COG0449 249 GYPHFMLKEIHEQPEAIRDTLRGRLD-EDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVE 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 400 LASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYT 479
Cdd:COG0449 328 IASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFT 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 480 SQFVSLVMFALMMCDDRISM-QERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALK 558
Cdd:COG0449 408 TQLAALYLLALYLARARGTLsAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALK 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 559 IKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVP 638
Cdd:COG0449 488 LKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADDVIEVP 567
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 54400724 639 HSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:COG0449 568 EVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-681 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 740.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 1 MCGIFAYLNyhvprtRREILETLIKGLQRLEYRGYDSAGVG-LDGGNdkdweanackIQLIKKKGKVKALDEEVHKQqdm 79
Cdd:PRK00331 1 MCGIVGYVG------QRNAAEILLEGLKRLEYRGYDSAGIAvLDDGG----------LEVRKAVGKVANLEAKLEEE--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 80 dldiEFDVHLGIAHTRWATHGEPSPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYM 159
Cdd:PRK00331 62 ----PLPGTTGIGHTRWATHGKPTERNAHPHT-DCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 160 YDnwesQDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtGKDkkgscgls 239
Cdd:PRK00331 137 LK----EGGDLLEAVRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGL-----------------GEG-------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 240 rvdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTARDhpgRAVQTLQMELQQIMKG 319
Cdd:PRK00331 188 ----------------ENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVE---REVYTVDWDASAAEKG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 320 NFSSFMQKEIFEQPESVVNTMRGRVNFDdytvnlGGLKDHIKEIQRCRRLILIACGTSYHAGMATRQVLEELTELPVMVE 399
Cdd:PRK00331 249 GYRHFMLKEIYEQPEAIRDTLEGRLDEL------GEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 400 LASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYT 479
Cdd:PRK00331 323 IASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFT 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 480 SQFVSLVMFALMMCDDRISM-QERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALK 558
Cdd:PRK00331 403 AQLAVLYLLALALAKARGTLsAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGALK 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 559 IKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDtETIKNTKRTIKVP 638
Cdd:PRK00331 483 LKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGD-EVAEEADDVIEVP 561
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 54400724 639 HSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:PRK00331 562 EVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-681 |
0e+00 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 725.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 1 MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGLDGGNDKDWEANACKIQ------LIKKKGKVKALDEEVH 74
Cdd:PTZ00394 1 MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDGTAASAptprpcVVRSVGNISQLREKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 75 KQQD----MDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTE 150
Cdd:PTZ00394 81 SEAVaatlPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSN-NGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 151 TIAKLVKYMYdnweSQD--VSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSehklstdhipilyrt 228
Cdd:PTZ00394 160 VISVLSEYLY----TRKgiHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIRR--------------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 229 GKDKKGSCGLSRVDsttclFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTARDHPGRAVQT 308
Cdd:PTZ00394 221 TDDRGCVMKLQTYD-----LTDLSGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRSIVKREVQH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 309 LQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDH-IKEIQRCRRLILIACGTSYHAGMATRQV 387
Cdd:PTZ00394 296 LDAKPEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQQsIRAILTSRRILFIACGTSLNSCLAVRPL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 388 LEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAG 467
Cdd:PTZ00394 376 FEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAG 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 468 PEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSM-DDEIQKLATELYHQKSVLIMGRG 546
Cdd:PTZ00394 456 VEVGVASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLGRG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 547 YHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTE 626
Cdd:PTZ00394 536 YDLATAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAE 615
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 54400724 627 TIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:PTZ00394 616 LKAAASEIVLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-681 |
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: 642.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 2 CGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVGLdggndkdweANACKIQLIKKKGKVKALDEEVhkqQDMDL 81
Cdd:TIGR01135 1 CGIVGYI------GQRDAVPILLEGLKRLEYRGYDSAGIAV---------VDEGKLFVRKAVGKVAELANKL---GEKPL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 82 DIEFdvhlGIAHTRWATHGEPSPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:TIGR01135 63 PGGV----GIGHTRWATHGKPTDENAHPHT-DEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 162 NwesqDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtGKDkkgscglsrv 241
Cdd:TIGR01135 138 E----GGDLLEAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGL-----------------GDG---------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 242 dsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHrikrtarDHPG----RAVQTLQMELQQIM 317
Cdd:TIGR01135 187 --------------ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIY-------NFEGapvqREVRVIDWDLDAAE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 318 KGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIqrcRRLILIACGTSYHAGMATRQVLEELTELPVM 397
Cdd:TIGR01135 246 KGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNI---DRIQIVACGTSYHAGLVAKYLIERLAGIPVE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 398 VELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKA 477
Cdd:TIGR01135 323 VEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKA 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 478 YTSQFVSLVMFALMMCDDR-ISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGA 556
Cdd:TIGR01135 403 FTTQLTVLYLLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGA 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 557 LKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIK 636
Cdd:TIGR01135 483 LKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIK 562
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 54400724 637 VPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:TIGR01135 563 LPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-680 |
3.71e-156 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 465.27 E-value: 3.71e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 1 MCGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVG-LDGGND------KDWEANACKIQLIKKKGKvkaldeEV 73
Cdd:PTZ00295 24 CCGIVGYL------GNEDASKILLEGIEILQNRGYDSCGIStISSGGElkttkyASDGTTSDSIEILKEKLL------DS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 74 HKQQdmdldiefdvHLGIAHTRWATHGEPSPVNSHPQrSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIA 153
Cdd:PTZ00295 92 HKNS----------TIGIAHTRWATHGGKTDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 154 KLVKYMYDNWESqdvsFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklSTDHIpilyrtgkdkk 233
Cdd:PTZ00295 161 NLIGLELDQGED----FQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGI------GDDSI----------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 234 gscglsrvdsttclfpveekaveyYFASDASAVIEHTNRVIFLEDDDVAAV-VDGRLSIHRIKRtardhpgraVQTLQME 312
Cdd:PTZ00295 220 ------------------------YVASEPSAFAKYTNEYISLKDGEIAELsLENVNDLYTQRR---------VEKIPEE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 313 LQQIMKGNFSSFMQKEIFEQPESVVNTM--RGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGMATRQVLEE 390
Cdd:PTZ00295 267 VIEKSPEPYPHWTLKEIFEQPIALSRALnnGGRLSGYNNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 391 LTEL-PVMVELASDF-LDRNTpvfRDDVCF-FISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAG 467
Cdd:PTZ00295 347 LKCFnTVQVIDASELtLYRLP---DEDAGViFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 468 PEIGVASTKAYTSQFVSLVMFALMMCDDR-ISMQE-RRKEIMLGLKRLPDLIKEVL-SMDDEIQKLATELYHQKSVLIMG 544
Cdd:PTZ00295 424 REVAVASTKAFTSQVTVLSLIALWFAQNKeYSCSNyKCSSLINSLHRLPTYIGMTLkSCEEQCKRIAEKLKNAKSMFILG 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 545 RGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKL--MPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDK 622
Cdd:PTZ00295 504 KGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQVKARGAYIIVITDD 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 54400724 623 EDtETIKNTKRTIKVPhSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTV 680
Cdd:PTZ00295 584 ED-LVKDFADEIILIP-SNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-284 |
1.27e-110 |
|
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: 332.49 E-value: 1.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 2 CGIFAYLNYhvprtrREILETLIKGLQRLEYRGYDSAGVGLDGGNdkdweanacKIQLIKKKGKVKALDEEVHKQqdmdl 81
Cdd:cd00714 1 CGIVGYIGK------REAVDILLEGLKRLEYRGYDSAGIAVIGDG---------SLEVVKAVGKVANLEEKLAEK----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 82 diEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNnEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:cd00714 61 --PLSGHVGIGHTRWATHGEPTDVNAHPHRSCDG-EIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 162 nwesQDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEhklstdhipilyrtgkdkkgscglsrv 241
Cdd:cd00714 138 ----GGLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGDG--------------------------- 186
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 54400724 242 dsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAV 284
Cdd:cd00714 187 --------------ENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
327-681 |
5.72e-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: 231.33 E-value: 5.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 327 KEIFEQPESVVNTmrgrvnFDDYTVNLGGLKDHIKEIQRcRRLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLD 406
Cdd:COG2222 2 REIAQQPEAWRRA------LAALAAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 407 RNTPVFRD-DVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSL 485
Cdd:COG2222 75 YPAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 486 VM-FALMMCDDrismqerrkEIMLGLKRLPDLIKEVLSMDDEIQKLAtELYHQKSVLIMGRGYHYATCLEGALKIKEITY 564
Cdd:COG2222 155 LAlLAAWGGDD---------ALLAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 565 MHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTEtikntkrtIKVPHSVDC- 643
Cdd:COG2222 225 GHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAA--------ITLPAIPDLh 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 54400724 644 --LQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:COG2222 297 daLDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
525-679 |
1.51e-68 |
|
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240142 [Multi-domain] Cd Length: 153 Bit Score: 220.98 E-value: 1.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 525 DEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQN 604
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54400724 605 ALQQVVARQGRPVVICDKEDTETIKNTkrTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVT 679
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDAKDLADV--VIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
368-493 |
1.69e-63 |
|
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: 206.58 E-value: 1.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 368 RLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGIT 447
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 54400724 448 NTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMC 493
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-282 |
1.56e-50 |
|
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: 175.33 E-value: 1.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 2 CGIFAYLNYHVPRTRReiLETLIKGLQRLEYRGYDSAGVGLDGGndkdweanackiqlikKKGKVKALDEEVHKQQDMDL 81
Cdd:cd00352 1 CGIFGIVGADGAASLL--LLLLLRGLAALEHRGPDGAGIAVYDG----------------DGLFVEKRAGPVSDVALDLL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 82 DIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:cd00352 63 DEPLKSGVALGHVRLATNGLPSEANAQPFRSE-DGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 162 NWEsqdvsFTTLVERVIQQLEGAFALVFKSVHfPGQAVGTRRG---SPLLIGVRSEHklstdhipilyrtgkdkkgscgl 238
Cdd:cd00352 142 EGG-----LFEAVEDALKRLDGPFAFALWDGK-PDRLFAARDRfgiRPLYYGITKDG----------------------- 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 54400724 239 srvdsttclfpveekavEYYFASDASAVIEHT-NRVIFLEDDDVA 282
Cdd:cd00352 193 -----------------GLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
362-491 |
4.52e-41 |
|
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: 145.90 E-value: 4.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 362 EIQRCRRLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDR-NTPVFRDDVCFFISQSGETADTLMGLRYCKERG 440
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 54400724 441 ALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALM 491
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
533-664 |
8.08e-33 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 122.79 E-value: 8.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 533 ELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQnALQQVVAR 612
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 54400724 613 QGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLR 664
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-212 |
5.59e-20 |
|
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: 89.83 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 2 CGIFA-YLNYHVPRTrreiletLIKGLQRLEYRGYDSAG-VGLDGGndkdweanacKIQLIKKKGKVkaldEEVHKQQDM 79
Cdd:cd00715 1 CGVFGiYGAEDAARL-------TYLGLYALQHRGQESAGiATSDGK----------RFHTHKGMGLV----SDVFDEEKL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 80 DldiEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKY 158
Cdd:cd00715 60 R---RLPGNIAIGHVRYSTAGSSSLENAQPFVVNSPLGGIALaHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIAR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 54400724 159 mydnwESQDVSFTTLVERVIQQLEGAFALVFksvhfpgqavGTRRGsplLIGVR 212
Cdd:cd00715 137 -----SLAKDDLFEAIIDALERVKGAYSLVI----------MTADG---LIAVR 172
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-189 |
1.26e-19 |
|
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: 92.39 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 1 MCGIFAYLNyhvprtRREILETLIKGLQRLEYRGYDSAG-VGLDGGndkdweanacKIQLIKKKGKVKaldeEVHKQQDM 79
Cdd:COG0034 7 ECGVFGIYG------HEDVAQLTYYGLYALQHRGQESAGiATSDGG----------RFHLHKGMGLVS----DVFDEEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 80 DldiEFDVHLGIAHTRWATHGEPSPVNSHP-QRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKY 158
Cdd:COG0034 67 E---RLKGNIAIGHVRYSTTGSSSLENAQPfYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIAR 143
|
170 180 190
....*....|....*....|....*....|.
gi 54400724 159 mydnwESQDVSFTTLVERVIQQLEGAFALVF 189
Cdd:COG0034 144 -----ELTKEDLEEAIKEALRRVKGAYSLVI 169
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-212 |
1.09e-17 |
|
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: 86.22 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 2 CGIFAYlNYHVPRTRREIletlIKGLQRLEYRGYDSAGVGLDGGNdkdweanacKIQLIKKKGKVKaldeEVHKQQDMDl 81
Cdd:TIGR01134 1 CGVVGI-YGQEEVAASLT----YYGLYALQHRGQESAGISVFDGN---------RFRLHKGNGLVS----DVFNEEHLQ- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 82 diEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMY 160
Cdd:TIGR01134 62 --RLKGNVGIGHVRYSTAGSSGLENAQPFVVNSPYGGLALaHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHND 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 54400724 161 dnwESQDVSFTTlVERVIQQLEGAFALVFKSVHF------PgqaVGTRrgsPLLIGVR 212
Cdd:TIGR01134 140 ---ESKDDLFDA-VARVLERVRGAYALVLMTEDGlvavrdP---HGIR---PLVLGRR 187
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-213 |
2.43e-16 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 82.42 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 1 MCGIFAYlnYHVPRTRREILEtlikGLQRLEYRGYDSAG-VGLDGGndkdweanacKIQLIKKKGKVKaldeEVHKQQDM 79
Cdd:PLN02440 1 ECGVVGI--FGDPEASRLCYL----GLHALQHRGQEGAGiVTVDGN----------RLQSITGNGLVS----DVFDESKL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 80 DldiEFDVHLGIAHTRWATHGEPSPVNSHPqrsdknneFI---------VIHNGIITNYKDLKKFLESKGYDFESETDTE 150
Cdd:PLN02440 61 D---QLPGDIAIGHVRYSTAGASSLKNVQP--------FVanyrfgsigVAHNGNLVNYEELRAKLEENGSIFNTSSDTE 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54400724 151 TIAKLVKymydnwESQDVSFTTLVERVIQQLEGAFALVFKsvhFPGQAVGTR-----RgsPLLIGVRS 213
Cdd:PLN02440 130 VLLHLIA------ISKARPFFSRIVDACEKLKGAYSMVFL---TEDKLVAVRdphgfR--PLVMGRRS 186
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
368-459 |
5.78e-15 |
|
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: 71.45 E-value: 5.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 368 RLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDRNTPVFRDD-VCFFISQSGETADTLMGLRYCKERGALTVGI 446
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90
....*....|...
gi 54400724 447 TNTVGSSISRETD 459
Cdd:cd05710 81 TDDEDSPLAKLAD 93
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-188 |
2.94e-14 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 75.46 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 2 CGIF-AYLNyhvprTRREILETLIKGLQRLEYRGYDSAGVGLdggndkdweANACKIQLIKKKGKVkaldEEVHKQQDMD 80
Cdd:PRK05793 15 CGVFgVFSK-----NNIDVASLTYYGLYALQHRGQESAGIAV---------SDGEKIKVHKGMGLV----SEVFSKEKLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 81 ldiEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKym 159
Cdd:PRK05793 77 ---GLKGNSAIGHVRYSTTGASDLDNAQPLVANYKLGSIAIaHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIA-- 151
|
170 180
....*....|....*....|....*....
gi 54400724 160 ydnwESQDVSFTTLVERVIQQLEGAFALV 188
Cdd:PRK05793 152 ----RSAKKGLEKALVDAIQAIKGSYALV 176
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
90-189 |
4.33e-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: 69.26 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 90 GIAHTRWATHGEPS----PVNShpqrSDKNneFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkymYDNWEs 165
Cdd:pfam13522 13 ALGHVRLAIVDLPDagnqPMLS----RDGR--LVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL----YEEWG- 81
|
90 100
....*....|....*....|....
gi 54400724 166 qdvsfttlvERVIQQLEGAFALVF 189
Cdd:pfam13522 82 ---------EDCLERLRGMFAFAI 96
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-160 |
5.63e-14 |
|
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: 72.30 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 2 CGIFAYLNyhvpRTRREIL-ETLIKGLQRLEYRG-YDSAGVGLDGGND-------KDweanackIQLIKKKGkvkaLDEE 72
Cdd:cd01907 1 CGIFGIMS----KDGEPFVgALLVEMLDAMQERGpGDGAGFALYGDPDafvyssgKD-------MEVFKGVG----YPED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 73 VHKQQDMDldiEFDVHLGIAHTRWATHgepSPVN---SHPqrsdknneF-----IVIHNGIITNYKDLKKFLESKGYDFE 144
Cdd:cd01907 66 IARRYDLE---EYKGYHWIAHTRQPTN---SAVWwygAHP--------FsigdiAVVHNGEISNYGSNREYLERFGYKFE 131
|
170
....*....|....*.
gi 54400724 145 SETDTETIAKLVKYMY 160
Cdd:cd01907 132 TETDTEVIAYYLDLLL 147
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
109-188 |
3.27e-12 |
|
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: 63.69 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 109 PQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYdnwesqdvsfttlVERVIQQLEGAFALV 188
Cdd:pfam13537 15 PMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW-------------GEDCVDRLNGMFAFA 81
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
420-491 |
5.80e-11 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 64.03 E-value: 5.80e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54400724 420 ISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF--ALM 491
Cdd:PRK05441 138 IAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMIstGVM 213
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-188 |
9.65e-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: 62.19 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 2 CGIFAYLNYHVPRTRREILETLikgLQRLEYRGYDSAGvgldggndkdweanackiqlikkkgkvkaldeevhkqqdmdl 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERM---LDALAHRGPDGSG------------------------------------------ 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 82 dIEFDVHLGIAHTRWATHGepsPVNSH-PQRSDKNNeFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkymY 160
Cdd:cd00712 36 -IWIDEGVALGHRRLSIID---LSGGAqPMVSEDGR-LVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL----Y 106
|
170 180
....*....|....*....|....*...
gi 54400724 161 DNWEsqdvsfttlvERVIQQLEGAFALV 188
Cdd:cd00712 107 EEWG----------EDCLERLNGMFAFA 124
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-188 |
2.53e-10 |
|
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: 63.32 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 1 MCGIFAYLNYHVPRTRreilETLIKGLQRLEYRGYDSAGVGLDGgndkdweanackiqlikkkgkvkaldeevhkqqdmd 80
Cdd:COG0367 1 MCGIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGIWVDG------------------------------------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 81 ldiefdvHLGIAHTRWATHGEPSpvNSHpQ-RSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkym 159
Cdd:COG0367 41 -------GVALGHRRLSIIDLSE--GGH-QpMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA---- 106
|
170 180
....*....|....*....|....*....
gi 54400724 160 YDNWEsqdvsfttlvERVIQQLEGAFALV 188
Cdd:COG0367 107 YEEWG----------EDCLERLNGMFAFA 125
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
401-492 |
2.83e-10 |
|
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: 61.38 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 401 ASDFLDRNTPvfRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAY 478
Cdd:cd05007 108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAG 185
|
90
....*....|....*.
gi 54400724 479 TSQFVSLVMF--ALMM 492
Cdd:cd05007 186 TAQKLALNMLstAVMI 201
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
368-672 |
3.05e-10 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 62.33 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 368 RLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDrNTPVFRDDVCFFI--SQSGETADTLMGLRYCKERGALTVG 445
Cdd:PRK11382 46 RIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCD-NTPYRLDDRCAVIgvSDYGKTEEVIKALELGRACGALTAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 446 ITNTVGSSISRETDCGVHINAGPEIGVASTKAYTsqfVSLVMFAlmmcddRISMQERRKEIMLGLKRLPDLIKEVLSMDD 525
Cdd:PRK11382 125 FTKRADSPITSAAEFSIDYQADCIWEIHLLLCYS---VVLEMIT------RLAPNAEIGKIKNDLKQLPNALGHLVRTWE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 526 EIQKLATELYHQKSVL-------IMGRGYHyatclEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHT 598
Cdd:PRK11382 196 EKGRQLGELASQWPMIytvaagpLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDES 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54400724 599 YAKCQNALQQVVARQGRPVVICDKEDTETIKntkrtikvphsvDCLQGILSVIPLQLLAFHLAVLRGYDVDFPR 672
Cdd:PRK11382 271 RHTTERAINFVKQRTDNVIVIDYAEISQGLH------------PWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
369-447 |
7.91e-10 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 55.84 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 369 LILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDRNTPVF--RDDVCFFISQSGETADTLMGLRYCKERGALTVGI 446
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 54400724 447 T 447
Cdd:cd04795 81 T 81
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
360-487 |
8.91e-10 |
|
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: 57.24 E-value: 8.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 360 IKEIQRCRRLILIACGTSYHAG--MATRqvleeLTELPVMVELASD---FLDRNTPVFRDDVCFFISQSGETADTLMGLR 434
Cdd:cd05013 7 VDLLAKARRIYIFGVGSSGLVAeyLAYK-----LLRLGKPVVLLSDphlQLMSAANLTPGDVVIAISFSGETKETVEAAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 54400724 435 YCKERGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVM 487
Cdd:cd05013 82 IAKERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
401-491 |
2.67e-09 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 58.95 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 401 ASDFLDRN-TPvfrDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIgVA-ST--K 476
Cdd:COG2103 122 AADLKALGlGP---GDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEV-ITgSTrlK 197
|
90
....*....|....*..
gi 54400724 477 AYTSQFVSLVMF--ALM 491
Cdd:COG2103 198 AGTAQKLVLNMLstAAM 214
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
360-493 |
2.21e-08 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 56.09 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 360 IKEIQRCRRLILIACGTSYHAGMATRQVLEEL----TELPVMVELASDFLDRNTPvfrDDVCFFISQSGETADTLMGLRY 435
Cdd:COG1737 128 VDLLAKARRIYIFGVGASAPVAEDLAYKLLRLgknvVLLDGDGHLQAESAALLGP---GDVVIAISFSGYTRETLEAARL 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 54400724 436 CKERGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVMF-ALMMC 493
Cdd:COG1737 205 AKERGAKVIAITDSPLSPLAKLAD--VVLYVPSEEPTLRSSAFSSRVAQLALIdALAAA 261
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
413-493 |
5.23e-08 |
|
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.
Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 51.77 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 413 RDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETD----CGVHINAGPeIGVASTkayTSQFVSLVMF 488
Cdd:cd05014 47 PGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDvvldLPVEEEACP-LGLAPT---TSTTAMLALG 122
|
....*.
gi 54400724 489 -ALMMC 493
Cdd:cd05014 123 dALAVA 128
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
120-189 |
4.75e-07 |
|
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: 52.72 E-value: 4.75e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 120 VIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkymYDNWEsqdvsfttlvERVIQQLEGAFALVF 189
Cdd:TIGR01536 70 IVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHL----YEEWG----------EECVDRLDGMFAFAL 125
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
88-182 |
1.01e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 50.35 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 88 HLGIAHTRWATHGEPSPVNSHPQRSDknnEFIVIHNGIITNYKDLKKFLESKGYDF-----ESETDTETIAKLvkyMYDN 162
Cdd:COG0121 77 RLVIAHVRKATVGPVSLENTHPFRGG---RWLFAHNGQLDGFDRLRRRLAEELPDElyfqpVGTTDSELAFAL---LLSR 150
|
90 100
....*....|....*....|
gi 54400724 163 WESQDVSFTTLVERVIQQLE 182
Cdd:COG0121 151 LRDGGPDPAEALAEALRELA 170
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
413-493 |
3.07e-06 |
|
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440557 [Multi-domain] Cd Length: 317 Bit Score: 49.59 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 413 RDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDcgVHINAGPE-----IGVASTkayTSQFVSLVM 487
Cdd:COG0794 91 PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAAD--VVLDLPVEreacpLNLAPT---TSTTATLAL 165
|
....*..
gi 54400724 488 F-ALMMC 493
Cdd:COG0794 166 GdALAVA 172
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-273 |
7.78e-06 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 49.14 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 1 MCGIFAYLNYH--VPRTRREILEtlikGLQRLEYRGYDSAGVGLDGGndkdweanackiqlikkkgkvkaldeevhkqqd 78
Cdd:PRK09431 1 MCGIFGILDIKtdADELRKKALE----MSRLMRHRGPDWSGIYASDN--------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 79 mdldiefdvhlGI-AHTRWA----THGEPSPVNShpqrsDKNNefIVIHNGIITNYKDLKKFLESKgYDFESETDTETIA 153
Cdd:PRK09431 44 -----------AIlGHERLSivdvNGGAQPLYNE-----DGTH--VLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVIL 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 154 KLvkymydnWESQDVSFttlvervIQQLEGAFALVfksvhfpgqavgtrrgspLLIGVRSEHKLSTDHIPI--LYrTGKD 231
Cdd:PRK09431 105 AL-------YQEKGPDF-------LDDLDGMFAFA------------------LYDSEKDAYLIARDPIGIipLY-YGYD 151
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 54400724 232 KKGscglsrvdsttclfpveekavEYYFASDASAVIEHTNRV 273
Cdd:PRK09431 152 EHG---------------------NLYFASEMKALVPVCKTI 172
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-188 |
1.13e-05 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 48.56 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 1 MCGIFAYLNYhvpRTRREILETLIKGL-QRLEYRGYDSAGVgldggndkdweanackiqlikkkgkvkaldeevhkqqdM 79
Cdd:PTZ00077 1 MCGILAIFNS---KGERHELRRKALELsKRLRHRGPDWSGI--------------------------------------I 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 80 DLDIEFDVHLGIAHTRWATHGepsPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkym 159
Cdd:PTZ00077 40 VLENSPGTYNILAHERLAIVD---LSDGKQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHL---- 112
|
170 180
....*....|....*....|....*....
gi 54400724 160 YDNWESQDvsfttlverVIQQLEGAFALV 188
Cdd:PTZ00077 113 YKEYGPKD---------FWNHLDGMFATV 132
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
414-488 |
3.11e-05 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 46.22 E-value: 3.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 54400724 414 DDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF 488
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
88-155 |
3.17e-05 |
|
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: 46.23 E-value: 3.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 54400724 88 HLGIAHTRWATHGEPSPVNSHPQRSDknnEFIVIHNGIITNYKDLKKFLESKGYDF-ESETDTETIAKL 155
Cdd:cd01908 81 PLVLAHVRAATVGPVSLENCHPFTRG---RWLFAHNGQLDGFRLLRRRLLRLLPRLpVGTTDSELAFAL 146
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
540-622 |
5.79e-04 |
|
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: 39.28 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400724 540 VLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGP-LALVDKLMPVIMIIMRdHTYAKCQNALQQVVARQGRPVV 618
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYS-GRTEELLAALEIAKELGIPVIA 79
|
....
gi 54400724 619 ICDK 622
Cdd:cd04795 80 ITDA 83
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
414-459 |
6.35e-03 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 38.97 E-value: 6.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 54400724 414 DDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETD 459
Cdd:PRK11337 188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLAD 233
|
|
| |
