|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-609 |
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: 1031.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 1 MCGIVAAVAQRDVAPLLIAGLKALEYRGYDSSGVAVLDHGAIRRVRAKGKVREMEALYLADPLPGGTGIAHTRWATHGVP 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 81 SEANAHPHI--AGRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQGMRLRAAVLATVRELEGAYAI 158
Cdd:COG0449 81 SDENAHPHTscSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 159 AVISGDEPGRVVGARRGAPLLVGLGIGENFLGSDAQALIQVTNKMLHLDENDVVEITRDSVQVFALDGTPVVRPVHESEL 238
Cdd:COG0449 161 AVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVDW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 239 STDAVERGEYRHYMQKEIFEQPRAIADTLEARLGAHG-VLPNIFGIDsDALLRKVRGLHIIACGTSYHAGLVAKYWIEEY 317
Cdd:COG0449 241 DAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGrVVLDELNLA-AEDLRNIDRIYIVACGTSYHAGLVGKYLIEEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 318 ARLPVSVEVASEYRYRETVVPEGTLFVAISQSGETADTLAAMRESRRRGyLGTLAICNVPESSVVREADLKLMTRAGPEI 397
Cdd:COG0449 320 ARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGPEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 398 GVASTKAFTTQLAGLALLTLELARRNG-LADDRYAALCAELQHLPRAVENALQLEPAIIVLAADFIHRQHALFLGRGVQY 476
Cdd:COG0449 399 GVASTKAFTTQLAALYLLALYLARARGtLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 477 PVALEGALKLKEISYIHAEAYAAGELKHGPLALVDENMPVIAVAPNGPLLDKLKSNLQEVRARGGRLIVFAD-GAAGMDD 555
Cdd:COG0449 479 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADeGDEEVEE 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 653309337 556 MAGHgaMLRVESGGSFIAPAVFTVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 609
Cdd:COG0449 559 LADD--VIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-609 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 988.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 1 MCGIVAAVAQRDVAPLLIAGLKALEYRGYDSSGVAVLDHGAIRRVRAKGKVREMEALYLADPLPGGTGIAHTRWATHGVP 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 81 SEANAHPHI--AGRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQGMRLRAAVLATVRELEGAYAI 158
Cdd:PRK00331 81 TERNAHPHTdcSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 159 AVISGDEPGRVVGARRGAPLLVGLGIGENFLGSDAQALIQVTNKMLHLDENDVVEITRDSVQVFALDGTPVVRPVHESEL 238
Cdd:PRK00331 161 AVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVDW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 239 STDAVERGEYRHYMQKEIFEQPRAIADTLEARLGAHGVLPNIfgidsDALLRKVRGLHIIACGTSYHAGLVAKYWIEEYA 318
Cdd:PRK00331 241 DASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDELGEGELA-----DEDLKKIDRIYIVACGTSYHAGLVAKYLIESLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 319 RLPVSVEVASEYRYRETVVPEGTLFVAISQSGETADTLAAMRESRRRGyLGTLAICNVPESSVVREADLKLMTRAGPEIG 398
Cdd:PRK00331 316 GIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELG-AKTLAICNVPGSTIARESDAVLYTHAGPEIG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 399 VASTKAFTTQLAGLALLTLELARRNG-LADDRYAALCAELQHLPRAVENALQLEPAIIVLAADFIHRQHALFLGRGVQYP 477
Cdd:PRK00331 395 VASTKAFTAQLAVLYLLALALAKARGtLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 478 VALEGALKLKEISYIHAEAYAAGELKHGPLALVDENMPVIAVAPNGPLLDKLKSNLQEVRARGGRLIVFADGAAGMDDMA 557
Cdd:PRK00331 475 VALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEVAEEA 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 653309337 558 GHgaMLRVESGGSFIAPAVFTVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 609
Cdd:PRK00331 555 DD--VIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-609 |
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: 862.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 2 CGIVAAVAQRDVAPLLIAGLKALEYRGYDSSGVAVLDHGAIRRVRAKGKVREMEALYLADPLPGGTGIAHTRWATHGVPS 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 82 EANAHPHI--AGRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQGMRLRAAVLATVRELEGAYAIA 159
Cdd:TIGR01135 81 DENAHPHTdeGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 160 VISGDEPGRVVGARRGAPLLVGLGIGENFLGSDAQALIQVTNKMLHLDENDVVEITRDSVQVFALDGTPVVRPVHESELS 239
Cdd:TIGR01135 161 VLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDWD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 240 TDAVERGEYRHYMQKEIFEQPRAIADTLEARLGAHGVLPNIFGIDSdaLLRKVRGLHIIACGTSYHAGLVAKYWIEEYAR 319
Cdd:TIGR01135 241 LDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEE--LLKNIDRIQIVACGTSYHAGLVAKYLIERLAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 320 LPVSVEVASEYRYRETVVPEGTLFVAISQSGETADTLAAMRESRRRGyLGTLAICNVPESSVVREADLKLMTRAGPEIGV 399
Cdd:TIGR01135 319 IPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELG-AKTLGICNVPGSTLVREADHTLYTRAGPEIGV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 400 ASTKAFTTQLAGLALLTLELARRNGLADDRYAA-LCAELQHLPRAVENALQLEPAIIVLAADFIHRQHALFLGRGVQYPV 478
Cdd:TIGR01135 398 ASTKAFTTQLTVLYLLALALAKARGTLSAEEEAeLVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 479 ALEGALKLKEISYIHAEAYAAGELKHGPLALVDENMPVIAVAPNGPLLDKLKSNLQEVRARGGRLIVFADGAAgmDDMAG 558
Cdd:TIGR01135 478 ALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDD--ETIAS 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 653309337 559 HGA-MLRVESGGSFIAPAVFTVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 609
Cdd:TIGR01135 556 VADdVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-609 |
3.29e-163 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 482.33 E-value: 3.29e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 1 MCGIVAAV------AQRDVAPLLIAGLKALEYRGYDSSGVAVLDHGAIRR-----VRAKGKVREMEA----------LYL 59
Cdd:PLN02981 1 MCGIFAYLnynvprERRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLESssplvFREEGKIESLVRsvyeevaetdLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 60 ADPLPGGTGIAHTRWATHGVPSEANAHPHIAG---RVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVL----ID 132
Cdd:PLN02981 81 DLVFENHAGIAHTRWATHGPPAPRNSHPQSSGpgnEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLakfvFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 133 RhLSQGMR---LRAAVLATVRELEGAYAIAVISGDEPGRVVGARRGAPLLVG---LGIGEN------------------- 187
Cdd:PLN02981 161 K-LNEEEGdvtFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGvkeLPEEKNssavftsegfltknrdkpk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 188 --FLGSDAQALIQVTNKMLHLDENDVVEITRDSVQVFALD------GTPVVRPVH-ESELSTDAVE-----RGEYRHYMQ 253
Cdd:PLN02981 240 efFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFEnekgrgGGGLSRPASvERALSTLEMEveqimKGNYDHYMQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 254 KEIFEQPRAIADTLEARL--GAHGVLPNIF-G--IDSDALLRKVRGLHIIACGTSYHAGLVAKYWIEEYARLPVSVEVAS 328
Cdd:PLN02981 320 KEIHEQPESLTTTMRGRLirGGSGKAKRVLlGglKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 329 EYRYRETVVPEGTLFVAISQSGETADTLAAMRESRRRGYLgTLAICNVPESSVVREADLKLMTRAGPEIGVASTKAFTTQ 408
Cdd:PLN02981 400 DLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGAL-CVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 409 LAGLALLTLELARRNGLADDRYAALCAELQHLPRAVENALQLEPAIIVLAADFIHRQHALFLGRGVQYPVALEGALKLKE 488
Cdd:PLN02981 479 IVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVKE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 489 ISYIHAEAYAAGELKHGPLALVDENMPVIAVAPNGPLLDKLKSNLQEVRARGGRLIVFA-DGAAGMDDMAGHGAMLRVES 567
Cdd:PLN02981 559 VALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICsKGDASSVCPSGGCRVIEVPQ 638
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 653309337 568 GGSFIAPAVFTVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 609
Cdd:PLN02981 639 VEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-608 |
5.31e-150 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 446.78 E-value: 5.31e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 1 MCGIVAAVAQRDVAPLLIAGLKALEYRGYDSSGVAVLDHG----------------AIRRVRAKgkvremealyLADPLP 64
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGgelkttkyasdgttsdSIEILKEK----------LLDSHK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 65 GGT-GIAHTRWATHGVPSEANAHPHI--AGRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQGMRL 141
Cdd:PTZ00295 94 NSTiGIAHTRWATHGGKTDENAHPHCdyKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 142 RAAVLATVRELEGAYAIAVISGDEPGRVVGARRGAPLLVGLGIGENFLGSDAQALIQVTNKMLHLDENDVVEITRDSVQV 221
Cdd:PTZ00295 174 QEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVND 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 222 FaLDGTPVVRPVHESELSTDAvergEYRHYMQKEIFEQPRAIADTLE--ARLGAHGVLPNIFGIDS-DALLRKVRGLHII 298
Cdd:PTZ00295 254 L-YTQRRVEKIPEEVIEKSPE----PYPHWTLKEIFEQPIALSRALNngGRLSGYNNRVKLGGLDQyLEELLNIKNLILV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 299 ACGTSYHAGLVAKYwIEEYARLPVSVEV--ASE---YRYREtvvPEGTlFVAISQSGETADTLAAMRESRRRGYLgTLAI 373
Cdd:PTZ00295 329 GCGTSYYAALFAAS-IMQKLKCFNTVQVidASEltlYRLPD---EDAG-VIFISQSGETLDVVRALNLADELNLP-KISV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 374 CNVPESSVVREADLKLMTRAGPEIGVASTKAFTTQLAGLALLTLELA--RRNGLADDRYAALCAELQHLPRAVENALQLE 451
Cdd:PTZ00295 403 VNTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAqnKEYSCSNYKCSSLINSLHRLPTYIGMTLKSC 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 452 PAII-VLAADFIHRQHALFLGRGVQYPVALEGALKLKEISYIHAEAYAAGELKHGPLALVDE--NMPVIAVAPNGPLLDK 528
Cdd:PTZ00295 483 EEQCkRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKekNTPVILIILDDEHKEL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 529 LKSNLQEVRARGGRLIVFADGAagmdDMAGHGA--MLRVESGGSfIAPAVFTVPLQLLAYHVAVLRGTDVDQPRNLAKSV 606
Cdd:PTZ00295 563 MINAAEQVKARGAYIIVITDDE----DLVKDFAdeIILIPSNGP-LTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTV 637
|
..
gi 653309337 607 TV 608
Cdd:PTZ00295 638 TV 639
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-609 |
5.08e-135 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 409.65 E-value: 5.08e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 1 MCGIVAAVAQ------RDVAPLLIAGLKALEYRGYDSSGVAV------------------LDHGAIRRVRAKGKVREM-- 54
Cdd:PTZ00394 1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAIdanigsekedgtaasaptPRPCVVRSVGNISQLREKvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 55 --EALYLADPLPGGT----GIAHTRWATHGVPSEANAHPHIA--GRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEV 126
Cdd:PTZ00394 81 seAVAATLPPMDATTshhvGIAHTRWATHGGVCERNCHPQQSnnGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 127 MAVLIDRHLSQGMRLRAAVLAT--VRELEGAYAIAVISGDEPGRVVGARRGAPLLVGL---------------------G 183
Cdd:PTZ00394 161 ISVLSEYLYTRKGIHNFADLALevSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydltdlsG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 184 IGENFLGSDAQALIQVTNKMLHLDENDVVEITRDSVQVFALDGTP---VVRPVHESELSTDAVERGEYRHYMQKEIFEQP 260
Cdd:PTZ00394 241 PLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQrsiVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 261 RAIADTLEARLGAHGVLPNIFGIDSDAL--LRKVRGLHIIACGTSYHAGLVAKYWIEEYARLPVSVEVASEYRYRETVVP 338
Cdd:PTZ00394 321 ESVISSMHGRIDFSSGTVQLSGFTQQSIraILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 339 EGTLFVAISQSGETADTLAAMRESRRRGYLgTLAICNVPESSVVREADLKLMTRAGPEIGVASTKAFTTQLAGLALLTLE 418
Cdd:PTZ00394 401 RDDVCFFVSQSGETADTLMALQLCKEAGAM-CVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 419 LARRNGLADDRYAALCAELQHLPRAVENALQL-EPAIIVLAADFIHRQHALFLGRGVQYPVALEGALKLKEISYIHAEAY 497
Cdd:PTZ00394 480 LSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 498 AAGELKHGPLALVDENMPVIAVAPNGPLLDKLKSNLQEVRARGGRLIVFADgAAGMDDMAGHGAMLRVESGGSFIAPAVF 577
Cdd:PTZ00394 560 HSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFAT-EVDAELKAAASEIVLVPKTVDCLQCVVN 638
|
650 660 670
....*....|....*....|....*....|..
gi 653309337 578 TVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 609
Cdd:PTZ00394 639 VIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-214 |
1.05e-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: 330.56 E-value: 1.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 2 CGIVAAVAQRDVAPLLIAGLKALEYRGYDSSGVAVLDHGAIRRVRAKGKVREMEALYLADPLPGGTGIAHTRWATHGVPS 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 82 EANAHPHI--AGRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQGMRLRAAVLATVRELEGAYAIA 159
Cdd:cd00714 81 DVNAHPHRscDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYALA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 653309337 160 VISGDEPGRVVGARRGAPLLVGLGIGENFLGSDAQALIQVTNKMLHLDENDVVEI 214
Cdd:cd00714 161 VISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
254-609 |
6.36e-75 |
|
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441824 [Multi-domain] Cd Length: 336 Bit Score: 242.50 E-value: 6.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 254 KEIFEQPRAIADTLEArlgahgVLPNIFGIDSDALLRKVRGLHIIACGTSYHAGLVAKYWIEEYARLPVSVEVASEY-RY 332
Cdd:COG2222 2 REIAQQPEAWRRALAA------LAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvVY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 333 RETVVPEGTLFVAISQSGETADTLAAMRESRRRGYLgTLAICNVPESSVVREADLKLMTRAGPEIGVASTKAFTTQLAGL 412
Cdd:COG2222 76 PAYLKLEGTLVVAISRSGNSPEVVAALELAKARGAR-TLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 413 ALLTLELARRNGLAddryaalcAELQHLPRAVENALQLEPAIIVLAADFiHRQHALFLGRGVQYPVALEGALKLKEISYI 492
Cdd:COG2222 155 LALLAAWGGDDALL--------AALDALPAALEAALAADWPAAALAALA-DAERVVFLGRGPLYGLAREAALKLKELSAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 493 HAEAYAAGELKHGPLALVDENMPVIAVAPNGPLLDKLKSNLQEVRARGGRLIVFADGAAGMDDMAGhgamlrVESGGSFI 572
Cdd:COG2222 226 HAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPA------IPDLHDAL 299
|
330 340 350
....*....|....*....|....*....|....*..
gi 653309337 573 APAVFTVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 609
Cdd:COG2222 300 DPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
452-607 |
1.06e-62 |
|
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: 204.03 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 452 PAIIVLAADFIHRQHALFLGRGVQYPVALEGALKLKEISYIHAEAYAAGELKHGPLALVDENMPVIAVAPNGPLLDKLKS 531
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653309337 532 NLQEVRARGGRLIVFADGAagmDDMAGHGAMLRVESGGSFIAPAVFTVPLQLLAYHVAVLRGTDVDQPRNLAKSVT 607
Cdd:cd05009 81 LIKEVKARGAKVIVITDDG---DAKDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
295-420 |
6.26e-59 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 192.71 E-value: 6.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 295 LHIIACGTSYHAGLVAKYWIEEYARLPVSVEVASEYRYRETVVPEGTLFVAISQSGETADTLAAMRESRRRGYLgTLAIC 374
Cdd:cd05008 2 ILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAK-TVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 653309337 375 NVPESSVVREADLKLMTRAGPEIGVASTKAFTTQLAGLALLTLELA 420
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-202 |
2.10e-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: 192.28 E-value: 2.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 2 CGIVAAVAQRDVAPLLI----AGLKALEYRGYDSSGVAVLDHGAIRRVRAKGKVREMEALYLADPLPGGTGIAHTRWATH 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLllllRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 78 GVPSEANAHPHI--AGRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQGmRLRAAVLATVRELEGA 155
Cdd:cd00352 81 GLPSEANAQPFRseDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREG-GLFEAVEDALKRLDGP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 653309337 156 YAIAVISGDePGRVVGARRGA---PLLVGLGI-GENFLGSDAQALIQVTNK 202
Cdd:cd00352 160 FAFALWDGK-PDRLFAARDRFgirPLYYGITKdGGLVFASEPKALLALPFK 209
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-173 |
8.82e-37 |
|
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: 142.85 E-value: 8.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 1 MCGIVAAVAQRDVAPLLIAGLKALEYRGYDSSGVAVLDHGAIRRVRAKGKVRE------MEAlyladpLPGGTGIAHTRW 74
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDvfdeedLER------LKGNIAIGHVRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 75 ATHGVPSEANAHPHIA----GRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQGmRLRAAVLATVR 150
Cdd:COG0034 81 STTGSSSLENAQPFYVnspfGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTKE-DLEEAIKEALR 159
|
170 180
....*....|....*....|...
gi 653309337 151 ELEGAYAIAVISGDepgRVVGAR 173
Cdd:COG0034 160 RVKGAYSLVILTGD---GLIAAR 179
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-196 |
1.21e-33 |
|
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: 128.73 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 2 CGIVAAVAQRDVAPLLIAGLKALEYRGYDSSGVAVLDHGAIRRVRAKGKVREM---EALylaDPLPGGTGIAHTRWATHG 78
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVfdeEKL---RRLPGNIAIGHVRYSTAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 79 VPSEANAHPHIA----GRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQGmRLRAAVLATVRELEG 154
Cdd:cd00715 78 SSSLENAQPFVVnsplGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAKD-DLFEAIIDALERVKG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 653309337 155 AYAIAVISGDepgRVVGAR-----RgaPLLVG-LGIGENFLGSDAQAL 196
Cdd:cd00715 157 AYSLVIMTAD---GLIAVRdphgiR--PLVLGkLEGDGYVVASESCAL 199
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
288-417 |
8.38e-29 |
|
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: 111.24 E-value: 8.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 288 LLRKVRGLHIIACGTSYHAGLVAKYWIEEYARLPVSVEVASEYRYRE-TVVPEGTLFVAISQSGETADTLAAMRESRRRG 366
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVlALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 653309337 367 yLGTLAICNVPESSVVREADLKLMTRAGPEIGVASTKAFTTQLAGLALLTL 417
Cdd:pfam01380 81 -AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAV 130
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-173 |
2.71e-27 |
|
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273461 [Multi-domain] Cd Length: 442 Bit Score: 115.11 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 2 CGIVAAVAQRDVAP-LLIAGLKALEYRGYDSSGVAVLDHGAIRRVRAKGKVREMEALYLADPLPGGTGIAHTRWATHGVP 80
Cdd:TIGR01134 1 CGVVGIYGQEEVAAsLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 81 SEANAHPHI----AGRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQGMRLRAAVLATVRELEGAY 156
Cdd:TIGR01134 81 GLENAQPFVvnspYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRGAY 160
|
170
....*....|....*..
gi 653309337 157 AIAVISGDepgRVVGAR 173
Cdd:TIGR01134 161 ALVLMTED---GLVAVR 174
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
461-592 |
5.75e-24 |
|
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: 97.37 E-value: 5.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 461 FIHRQHALFLGRGVQYPVALEGALKLKEISYIHAEAYAAGELKHGPLALVDENMPVIAVAPNGPLLDKLKsNLQEVRARG 540
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 653309337 541 GRLIVFADGAAG-MDDMAGHGAMLRVESGgsFIAPAVFTVPLQLLAYHVAVLR 592
Cdd:pfam01380 81 AKIIAITDSPGSpLAREADHVLYINAGPE--TGVASTKSITAQLAALDALAVA 131
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-196 |
3.45e-23 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 102.80 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 2 CGIVAAVA--QRDVAPLLIAGLKALEYRGYDSSGVAVLDHGAIRRVRAKGKVREMEALYLADPLPGGTGIAHTRWATHGV 79
Cdd:PRK05793 15 CGVFGVFSknNIDVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 80 PSEANAHPHIA----GRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQGmrLRAAVLATVRELEGA 155
Cdd:PRK05793 95 SDLDNAQPLVAnyklGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKG--LEKALVDAIQAIKGS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 653309337 156 YAIAVISGDepgRVVGAR-----RgaPLLVGLGIGENFLGSDAQAL 196
Cdd:PRK05793 173 YALVILTED---KLIGVRdphgiR--PLCLGKLGDDYILSSESCAL 213
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-173 |
3.49e-22 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 100.14 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 1 MCGIVAAVAQRDVAPLLIAGLKALEYRGYDSSGVAVLDHGAIRRVRAKGKVREMEALYLADPLPGGTGIAHTRWATHGVP 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 81 SEANAHPHIA----GRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQgmRLRAAVLATVRELEGAY 156
Cdd:PLN02440 81 SLKNVQPFVAnyrfGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKAR--PFFSRIVDACEKLKGAY 158
|
170
....*....|....*..
gi 653309337 157 AIAVISGDepgRVVGAR 173
Cdd:PLN02440 159 SMVFLTED---KLVAVR 172
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
65-173 |
5.98e-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: 433279 [Multi-domain] Cd Length: 130 Bit Score: 80.43 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 65 GGTGIAHTRWATHGVPSEANaHPHI--AGRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQgmrlr 142
Cdd:pfam13522 10 GGVALGHVRLAIVDLPDAGN-QPMLsrDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEWGED----- 83
|
90 100 110
....*....|....*....|....*....|.
gi 653309337 143 aavlaTVRELEGAYAIAVISgDEPGRVVGAR 173
Cdd:pfam13522 84 -----CLERLRGMFAFAIWD-RRRRTLFLAR 108
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-196 |
7.79e-16 |
|
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: 77.31 E-value: 7.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 2 CGIVAAV---AQRDVAPLLIAGLKALEYRG-YDSSGVAVLDHGAIRRV---------RAKGKVREMEALYLADPLPGGTG 68
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDAFVYssgkdmevfKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 69 IAHTRWATHGVPSEANAHPHIAGRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQG---MRLRAAV 145
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPFSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGglpLEYYKHI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653309337 146 LATVRE----------------LEGAYAIAVISGDEPGRVVGARRGAPLLVGLGIGENFLGSDAQAL 196
Cdd:cd01907 161 IRMPEEerelllalrltyrladLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAI 227
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-216 |
3.35e-15 |
|
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: 74.90 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 2 CGIVAAVAQRDVAP---LLIAGLKALEYRGYDSSGVAVLdhgairrvrakgkvremealyladplpGGTGIAHTRWAThg 78
Cdd:cd00712 1 CGIAGIIGLDGASVdraTLERMLDALAHRGPDGSGIWID---------------------------EGVALGHRRLSI-- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 79 VPSEANAHPHI--AGRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHlsqGmrlraavLATVRELEGAY 156
Cdd:cd00712 52 IDLSGGAQPMVseDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEEW---G-------EDCLERLNGMF 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653309337 157 AIAVISGDEpGRVVGAR-----RgaPLLVGLGiGENFL-GSDAQALIQVTNKMLHLDENDVVEITR 216
Cdd:cd00712 122 AFALWDKRK-RRLFLARdrfgiK--PLYYGRD-GGGLAfASELKALLALPGVPRELDEAALAEYLA 183
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
59-153 |
6.96e-13 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 68.84 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 59 LADPLPGGTGIAHTRWATHGVPSEANAHPHIAGRVAIVHNGIIENYAGLRAGLQA---DGHVFT--SETDTEVMAVLIDR 133
Cdd:COG0121 70 LARPIKSRLVIAHVRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLAEelpDELYFQpvGTTDSELAFALLLS 149
|
90 100
....*....|....*....|.
gi 653309337 134 HLSQ-GMRLRAAVLATVRELE 153
Cdd:COG0121 150 RLRDgGPDPAEALAEALRELA 170
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-173 |
2.08e-12 |
|
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: 69.87 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 1 MCGIVAAVAQRDVA--PLLIAGLKALEYRGYDSSGVAVLDHGAIrrvrakgkvremealyladplpggtgiAHTRWAThg 78
Cdd:COG0367 1 MCGIAGIIDFDGGAdrEVLERMLDALAHRGPDGSGIWVDGGVAL---------------------------GHRRLSI-- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 79 VPSEANAH-PHIA--GRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHlsqGmrlraavLATVRELEGA 155
Cdd:COG0367 52 IDLSEGGHqPMVSedGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEEW---G-------EDCLERLNGM 121
|
170
....*....|....*...
gi 653309337 156 YAIAVISGDEpGRVVGAR 173
Cdd:COG0367 122 FAFAIWDRRE-RRLFLAR 138
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
71-198 |
4.33e-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: 63.31 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 71 HTRWAThgVPSEANAHPHIA---GRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHlsqgmrlraAVLA 147
Cdd:pfam13537 1 HRRLSI--IDLEGGAQPMVSsedGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAE---------WGED 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 653309337 148 TVRELEGAYAIAVISGDEpGRVVGAR-RGA--PLLVGLGIGENFL-GSDAQALIQ 198
Cdd:pfam13537 70 CVDRLNGMFAFAIWDRRR-QRLFLARdRFGikPLYYGRDDGGRLLfASELKALLA 123
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
33-161 |
2.49e-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: 64.33 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 33 GVAVLD--HGAIRRVRAKGKVREMEALY-LADPLPGGTGIAHTRWATHGVPSEANAHPHIAGRVAIVHNGIIENYAGLRA 109
Cdd:cd01908 45 GIGWYEgkGGRPFRYRSPLPAWSDINLEsLARPIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRLLRR 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 653309337 110 GL-QADGHVFTSETDTEVMAVLI-----DRHLSQGMRLRAAVLATVRELEGAYAIAVI 161
Cdd:cd01908 125 RLlRLLPRLPVGTTDSELAFALLlsrllERDPLDPAELLDAILQTLRELAALAPPGRL 182
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
298-386 |
2.23e-08 |
|
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: 52.58 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 298 IACGTSYHAGLVAKYWIEEYARLPVSVEVASEYRYRETV-VPEGTLFVAISQSGETADTLAAMRESRRRGYLgTLAICNV 376
Cdd:cd05710 5 VGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKrLTEKSVVILASHSGNTKETVAAAKFAKEKGAT-VIGLTDD 83
|
90
....*....|
gi 653309337 377 PESSVVREAD 386
Cdd:cd05710 84 EDSPLAKLAD 93
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
287-415 |
6.37e-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: 51.85 E-value: 6.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 287 ALLRKVRGLHIIACGTSyhaGLVAKYWIEEYARLPVSVEVASEYRYRETV---VPEGTLFVAISQSGETADTLAAMRESR 363
Cdd:cd05013 8 DLLAKARRIYIFGVGSS---GLVAEYLAYKLLRLGKPVVLLSDPHLQLMSaanLTPGDVVIAISFSGETKETVEAAEIAK 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 653309337 364 RRGyLGTLAICNVPESSVVREADLKLMTRAgpEIGVASTKAFTTQLAGLALL 415
Cdd:cd05013 85 ERG-AKVIAITDSANSPLAKLADIVLLVSS--EEGDFRSSAFSSRIAQLALI 133
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
287-424 |
1.48e-07 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 53.39 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 287 ALLRKVRGLHIIACGTSYHAGLVAKYWIEeYARLPVSVEVASEYRYRETV--VPEGTLFVAISQSGETADTLAAMRESRR 364
Cdd:COG1737 129 DLLAKARRIYIFGVGASAPVAEDLAYKLL-RLGKNVVLLDGDGHLQAESAalLGPGDVVIAISFSGYTRETLEAARLAKE 207
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 653309337 365 RGyLGTLAICNVPESSVVREADLKLMTRAGPEIGVAStkAFTTQLAGLAL---LTLELARRNG 424
Cdd:COG1737 208 RG-AKVIAITDSPLSPLAKLADVVLYVPSEEPTLRSS--AFSSRVAQLALidaLAAAVAQRDG 267
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
468-551 |
2.58e-07 |
|
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: 48.52 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 468 LFLGRGVQYPVALEGALKLKEISYIHAEAYAAGELKHGP-LALVDENMPVIAVAPNGpLLDKLKSNLQEVRARGGRLIVF 546
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYSG-RTEELLAALEIAKELGIPVIAI 80
|
....*
gi 653309337 547 ADGAA 551
Cdd:cd04795 81 TDALA 85
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
14-201 |
6.82e-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: 51.95 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 14 APLLIAGLKALEYRGYDSSGVAVLDHGAIRrvrakGKVRemeaLYLADPLPGGTGIAHTrwathgvpseanahphiAGRV 93
Cdd:TIGR01536 15 DEAIKRMSDTIAHRGPDASGIEYKDGNAIL-----GHRR----LAIIDLSGGAQPMSNE-----------------GKTY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 94 AIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHlsqGMRlraavlaTVRELEGAYAIAVISGdEPGRVVGAR 173
Cdd:TIGR01536 69 VIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLYEEW---GEE-------CVDRLDGMFAFALWDS-EKGELFLAR 137
|
170 180 190
....*....|....*....|....*....|.
gi 653309337 174 R--G-APLLVGLGIGENFLGSDAQALIQVTN 201
Cdd:TIGR01536 138 DrfGiKPLYYAYDGGQLYFASEIKALLAHPN 168
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
277-600 |
8.53e-07 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 51.16 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 277 LPNIFGIDSDALLRKVRGLHIIACGTSYHAGLVAKYWIEEYARLPVSV----EVASEYRYRetvVPEGTLFVAISQSGET 352
Cdd:PRK11382 29 VPLVHAIVEEMVKRDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAisgwEFCDNTPYR---LDDRCAVIGVSDYGKT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 353 ADTLAAMRESRRRGYLgTLAICNVPESSVVREADLKLMTRAGP--EIGVASTKAFTTQLAGLALLTLELAR-RNGLADdr 429
Cdd:PRK11382 106 EEVIKALELGRACGAL-TAAFTKRADSPITSAAEFSIDYQADCiwEIHLLLCYSVVLEMITRLAPNAEIGKiKNDLKQ-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 430 yaaLCAELQHLPRAVEN-ALQLE------PAIIVLAAdfihrqhalflgrGVQYPVAL-EGALKLKEISYIHAEAYAAGE 501
Cdd:PRK11382 183 ---LPNALGHLVRTWEEkGRQLGelasqwPMIYTVAA-------------GPLRPLGYkEGIVTLMEFTWTHGCVIESGE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 502 LKHGPLALVDENMPVIAVAPNGPLLDKLKSNLQEVRARGGRLIV--FADGAAGMDdmaghgamlrvesggSFIAPAVFTV 579
Cdd:PRK11382 247 FRHGPLEIVEPGVPFLFLLGNDESRHTTERAINFVKQRTDNVIVidYAEISQGLH---------------PWLAPFLMFV 311
|
330 340
....*....|....*....|.
gi 653309337 580 PLQLLAYHVAVLRGTDVDQPR 600
Cdd:PRK11382 312 PMEWLCYYLSIYKDHNPDERR 332
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-196 |
2.57e-06 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 50.48 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 1 MCGIVA---AVAQRD-VAPLLIAGLKALEYRGYDSSGVAVLDHGairrvrakgkvremealyladplPGGTGI-AHTRWA 75
Cdd:PTZ00077 1 MCGILAifnSKGERHeLRRKALELSKRLRHRGPDWSGIIVLENS-----------------------PGTYNIlAHERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 76 THGVPSEANAHPHIAGRVAIVHNGIIENYAGLRAGLQADGHVFTSETDTEVMAVLIDRHLSQGMrlraavlatVRELEGA 155
Cdd:PTZ00077 58 IVDLSDGKQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPKDF---------WNHLDGM 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 653309337 156 YAIaVISGDEPGRVVGARRG---APLLVGLGI-GENFLGSDAQAL 196
Cdd:PTZ00077 129 FAT-VIYDMKTNTFFAARDHigiIPLYIGYAKdGSIWFSSELKAL 172
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
336-410 |
1.16e-05 |
|
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: 45.23 E-value: 1.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653309337 336 VVPEGTLFVAISQSGETADTLAAMRESRRRGyLGTLAICNVPESSVVREADLKLMTRAGPE---IGVASTKAFTTQLA 410
Cdd:cd05014 44 MVTPGDVVIAISNSGETDELLNLLPHLKRRG-APIIAITGNPNSTLAKLSDVVLDLPVEEEacpLGLAPTTSTTAMLA 120
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
297-374 |
1.43e-05 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 43.52 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 297 IIACGTSYHAGLVAKYWIEEYARLPVSVEVASEYRYRETVVP--EGTLFVAISQSGETADTLAAMRESRRRGyLGTLAIC 374
Cdd:cd04795 3 VIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELG-IPVIAIT 81
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
344-408 |
2.47e-05 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 46.36 E-value: 2.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653309337 344 VAISQSGETADTLAAMRESRRRGYLgTLAICNVPESSVVREADLKLMTRAGPEIGVAST--KAFTTQ 408
Cdd:cd05007 123 IGIAASGRTPYVLGALRYARARGAL-TIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAGTAQ 188
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
344-408 |
9.22e-05 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 44.77 E-value: 9.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653309337 344 VAISQSGETADTLAAMRESRRRGYLgTLAICNVPESSVVREADLKLMTRAGPEIGVAST--KAFTTQ 408
Cdd:PRK05441 136 VGIAASGRTPYVIGALEYARERGAL-TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQ 201
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
469-599 |
3.18e-04 |
|
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: 41.46 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 469 FLGRGVQYPVALEGALKLKEIS--YIHAEAYAAGELKHGPLALVDENMPVIAVAPNGP--------LLDKLKSNLQevra 538
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPytrqydldLLKELRRDGI---- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653309337 539 rGGRLIVFADGA-AGMDDMAGHGAMLRVESGGSFIAPaVFTVPLQLLAYHVAVLRGTDVDQP 599
Cdd:cd05010 79 -AARVIAISPESdAGIEDNSHYYLPGSRDLDDVYLAF-PYILYAQLFALFNSIALGLTPDNP 138
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
301-366 |
5.48e-04 |
|
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.
Pssm-ID: 240148 [Multi-domain] Cd Length: 119 Bit Score: 39.94 E-value: 5.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653309337 301 GTSYHAGLVAKYWIEEYARLPVsvevaseYRYRETVVP----EGTLFVAISQSGETADTLAAMRESRRRG 366
Cdd:cd05017 8 GGSGIGGDLLESLLLDEAKIPV-------YVVKDYTLPafvdRKTLVIAVSYSGNTEETLSAVEQAKERG 70
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| CE4_RC0012_like |
cd10963 |
Putative catalytic NodB homology domain of uncharacterized protein RC0012 from Rickettsia ... |
252-303 |
1.96e-03 |
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Putative catalytic NodB homology domain of uncharacterized protein RC0012 from Rickettsia conorii and its bacterial homologs; This family contains an uncharacterized protein RC0012 from Rickettsia conorii and its bacterial homologs. Although their biochemical properties remain to be determined, members in this family seems to be composed of a seven-stranded barrel with detectable sequence similarity to the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily.
Pssm-ID: 200585 Cd Length: 182 Bit Score: 39.59 E-value: 1.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 653309337 252 MQKEIFEqpraiadtLEARLGAHGVLPNIF----GIDSD-ALLRKVRGLHIIACGTS 303
Cdd:cd10963 95 LNVEVLE--------TEKLLLENGILPSVFfrfpGLVSDkALMEKLRELGLIPLGAD 143
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