|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-717 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 892.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 1 MCGIFGYCNYLVERSRGEIIDTLVDGLQRLEYRGYDSTGIAIDGDEADSTF---IYKQIGKVSAL----KEEITKQNPNR 73
Cdd:PLN02981 1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLESSsplVFREEGKIESLvrsvYEEVAETDLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 74 DVTFVSHCGIAHTRWATHGRPEQVNCHPQRSDPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHLYN 153
Cdd:PLN02981 81 DLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 154 TNLQNGHDLDFHELTKLVLLELEGSYGLLCKSCHYPNEVIATRKGSPLLIGVKsekklkvdfvdvefpeenagqpEIPLK 233
Cdd:PLN02981 161 KLNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVK----------------------ELPEE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 234 SNNKSFglgpkkarefeagsqnanllpiaanefnlrhSQSRAFLSEDGSpTPVEFFVSSDAASVVKHTKKVLFLEDDDLA 313
Cdd:PLN02981 219 KNSSAV-------------------------------FTSEGFLTKNRD-KPKEFFLASDASAVVEHTKRVLVIEDNEVV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 314 HIYDGELHIHRSRREVG---------ASMTRSIQTLEMELAQIMKGPYDHFMQKEIYEQPESTFNTMRGRI----DYENN 380
Cdd:PLN02981 267 HLKDGGVGIYKFENEKGrgggglsrpASVERALSTLEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLirggSGKAK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 381 KVILGGLKAWLPVVRRARRLIMIACGTSYHSCLATRAIFEELSDIPVSVELASDFLDRKCPVFRDDVCVFVSQSGETADT 460
Cdd:PLN02981 347 RVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADT 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 461 MLALNYCLERGALTVGIVNSVGSSISRVTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLSDDRVSKIDRRIEIIQG 540
Cdd:PLN02981 427 LRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDG 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 541 LKLIPGQIKQVLKLEPRIKKLcATELKDQKSLLLLGRGYQFAAALEGALKIKEISYMHSEGVLAGELKHGVLALVDENLP 620
Cdd:PLN02981 507 LFDLPNKVREVLKLDQEMKEL-AELLIDEQSLLVFGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLP 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 621 IIAFGTRDSLFPKVVSSIEQVTARKGHPIIICNENDEVWAQKSKSIDLqtLEVPQTVDCLQGLINIIPLQLMSYWLAVNK 700
Cdd:PLN02981 586 IIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDASSVCPSGGCRV--IEVPQVEDCLQPVINIVPLQLLAYHLTVLR 663
|
730
....*....|....*..
gi 6322745 701 GIDVDFPRNLAKSVTVE 717
Cdd:PLN02981 664 GHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-717 |
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: 744.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 1 MCGIFGYCnylverSRGEIIDTLVDGLQRLEYRGYDSTGIA-IDGDEADstfIYKQIGKVSALKEEITKQNPNrdvtfvS 79
Cdd:COG0449 1 MCGIVGYI------GKRDAAPILLEGLKRLEYRGYDSAGIAvLDDGGLE---VRKAVGKLANLEEKLAEEPLS------G 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 80 HCGIAHTRWATHGRPEQVNCHPQRSDpEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAklylHLYNTNLQNG 159
Cdd:COG0449 66 TIGIGHTRWATHGAPSDENAHPHTSC-SGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIA----HLIEEYLKGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 160 HDLdfHELTKLVLLELEGSYGLLCKSCHYPNEVIATRKGSPLLIGVksekklkvdfvdvefpeenagqpeiplksnnksf 239
Cdd:COG0449 141 GDL--LEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL---------------------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 240 glgpkkarefeagsqnanllpiaanefnlrhsqsraflSEDgsptpvEFFVSSDAASVVKHTKKVLFLEDDDLAHIYDGE 319
Cdd:COG0449 185 --------------------------------------GEG------ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 320 LHIHRSRrevGASMTRSIQTLEMELAQIMKGPYDHFMQKEIYEQPESTFNTMRGRIDyENNKVILGGLKAWLPVVRRARR 399
Cdd:COG0449 221 VEIYDLD---GEPVEREVKTVDWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLD-EDGRVVLDELNLAAEDLRNIDR 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 400 LIMIACGTSYHSCLATRAIFEELSDIPVSVELASDFLDRKCPVFRDDVCVFVSQSGETADTMLALNYCLERGALTVGIVN 479
Cdd:COG0449 297 IYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICN 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 480 SVGSSISRVTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLSDDR-VSKIDRRIEIIQGLKLIPGQIKQVLKLEPRI 558
Cdd:COG0449 377 VVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAALYLLALYLARARgTLSAEEEAELLEELRKLPEKIEEVLDLEEQI 456
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 559 KKLcATELKDQKSLLLLGRGYQFAAALEGALKIKEISYMHSEGVLAGELKHGVLALVDENLPIIAFGTRDSLFPKVVSSI 638
Cdd:COG0449 457 EEL-AEKYADARNALFLGRGINYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNI 535
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322745 639 EQVTARKGHPIIICNENDEvwaqKSKSIDLQTLEVPQTVDCLQGLINIIPLQLMSYWLAVNKGIDVDFPRNLAKSVTVE 717
Cdd:COG0449 536 QEVKARGGKVIAIADEGDE----EVEELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-717 |
0e+00 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 690.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 1 MCGIFGYCNYLVERSRGEIIDTLVDGLQRLEYRGYDSTGIAID---------GDEADST----FIYKQIGKVSALKE--- 64
Cdd:PTZ00394 1 MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDanigsekedGTAASAPtprpCVVRSVGNISQLREkvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 65 --EITKQNPNRDVTFVSHCGIAHTRWATHGRPEQVNCHPQRSDpEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTE 142
Cdd:PTZ00394 81 seAVAATLPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSN-NGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 143 CIAKLYLHLYNTNlqngHDLDFHELTKLVLLELEGSYGLLCKSCHYPNEVIATRKGSPLLIGVKsekklkvdfvdvefpe 222
Cdd:PTZ00394 160 VISVLSEYLYTRK----GIHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIR---------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 223 enagqpeiplksNNKSFGLGpkkarefeAGSQNANLLPIAAnefnlrhsqsraflsedgsptPVEFFVSSDAASVVKHTK 302
Cdd:PTZ00394 220 ------------RTDDRGCV--------MKLQTYDLTDLSG---------------------PLEVFFSSDVNSFAEYTR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 303 KVLFLEDDDLAHIYDGELHIHRSRREVGASMTRSIQTLEMELAQIMKGPYDHFMQKEIYEQPESTFNTMRGRIDYENNKV 382
Cdd:PTZ00394 259 EVVFLEDGDIAHYCDGALRFYNAAERQRSIVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 383 ILGGLKAW-LPVVRRARRLIMIACGTSYHSCLATRAIFEELSDIPVSVELASDFLDRKCPVFRDDVCVFVSQSGETADTM 461
Cdd:PTZ00394 339 QLSGFTQQsIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTL 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 462 LALNYCLERGALTVGIVNSVGSSISRVTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLSDDRVSKIDRRIEIIQGL 541
Cdd:PTZ00394 419 MALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGL 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 542 KLIPGQIKQVLKLEPRIKKLCATELKDQKSLLLLGRGYQFAAALEGALKIKEISYMHSEGVLAGELKHGVLALVDENLPI 621
Cdd:PTZ00394 499 AELPAAISECLKITHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPV 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 622 IAFGTRDSLFPKVVSSIEQVTARKGHPIIICNEND-EVWAQKSKSIdlqtlEVPQTVDCLQGLINIIPLQLMSYWLAVNK 700
Cdd:PTZ00394 579 LAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDaELKAAASEIV-----LVPKTVDCLQCVVNVIPFQLLAYYMALLR 653
|
730
....*....|....*..
gi 6322745 701 GIDVDFPRNLAKSVTVE 717
Cdd:PTZ00394 654 GNNVDCPRNLAKSVTVQ 670
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-717 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 686.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 1 MCGIFGYCnylverSRGEIIDTLVDGLQRLEYRGYDSTGIA-IDGDEADstfIYKQIGKVSALKEEITKQNpnrdvtFVS 79
Cdd:PRK00331 1 MCGIVGYV------GQRNAAEILLEGLKRLEYRGYDSAGIAvLDDGGLE---VRKAVGKVANLEAKLEEEP------LPG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 80 HCGIAHTRWATHGRPEQVNCHPQRSDPEDqFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAklylHLYNTNLQNG 159
Cdd:PRK00331 66 TTGIGHTRWATHGKPTERNAHPHTDCSGR-IAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIA----HLIEEELKEG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 160 hdLDFHELTKLVLLELEGSYGLLCKSCHYPNEVIATRKGSPLLIGVksekklkvdfvdvefpeenagqpeiplksnnksf 239
Cdd:PRK00331 141 --GDLLEAVRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGL---------------------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 240 GLGpkkarefeagsqnanllpiaanefnlrhsqsraflsedgsptpvEFFVSSDAASVVKHTKKVLFLEDDDLAHIYDGE 319
Cdd:PRK00331 185 GEG--------------------------------------------ENFLASDALALLPYTRRVIYLEDGEIAVLTRDG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 320 LHIHRSRrevGASMTRSIQTLEMELAQIMKGPYDHFMQKEIYEQPESTFNTMRGRIDyennkvILGGLKAWLPVVRRARR 399
Cdd:PRK00331 221 VEIFDFD---GNPVEREVYTVDWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLD------ELGEGELADEDLKKIDR 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 400 LIMIACGTSYHSCLATRAIFEELSDIPVSVELASDFLDRKCPVFRDDVCVFVSQSGETADTMLALNYCLERGALTVGIVN 479
Cdd:PRK00331 292 IYIVACGTSYHAGLVAKYLIESLAGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICN 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 480 SVGSSISRVTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLSDDRVSKIDRRI-EIIQGLKLIPGQIKQVLKLEPRI 558
Cdd:PRK00331 372 VPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVLYLLALALAKARGTLSAEEEaDLVHELRELPALIEQVLDLKEQI 451
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 559 KKLcATELKDQKSLLLLGRGYQFAAALEGALKIKEISYMHSEGVLAGELKHGVLALVDENLPIIAFGTRDSLFPKVVSSI 638
Cdd:PRK00331 452 EEL-AEDFADARNALFLGRGVDYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNI 530
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322745 639 EQVTARKGHPIIICNENDEVWAqksksIDLQTLEVPQTVDCLQGLINIIPLQLMSYWLAVNKGIDVDFPRNLAKSVTVE 717
Cdd:PRK00331 531 QEVKARGARVIVIADEGDEVAE-----EADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-717 |
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: 599.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 2 CGIFGYcnyLVERSRGEIidtLVDGLQRLEYRGYDSTGIAIDGDeaDSTFIYKQIGKVSALKEEiTKQNPNRDVTfvshc 81
Cdd:TIGR01135 1 CGIVGY---IGQRDAVPI---LLEGLKRLEYRGYDSAGIAVVDE--GKLFVRKAVGKVAELANK-LGEKPLPGGV----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 82 GIAHTRWATHGRPEQVNCHPQRSDPEDqFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAklylHLYNTNLQNGHD 161
Cdd:TIGR01135 67 GIGHTRWATHGKPTDENAHPHTDEGGR-IAVVHNGIIENYAELREELEARGHVFSSDTDTEVIA----HLIEEELREGGD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 162 LDfhELTKLVLLELEGSYGLLCKSCHYPNEVIATRKGSPLLIGVKSEkklkvdfvdvefpeenagqpeiplksnnksfgl 241
Cdd:TIGR01135 142 LL--EAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGLGDG--------------------------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 242 gpkkarefeagsqnanllpiaanefnlrhsqsraflsedgsptpvEFFVSSDAASVVKHTKKVLFLEDDDLAHIYDGELH 321
Cdd:TIGR01135 187 ---------------------------------------------ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVE 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 322 IHRSRrevGASMTRSIQTLEMELAQIMKGPYDHFMQKEIYEQPESTFNTMRGRIDyENNKVILGGLKAWLpvVRRARRLI 401
Cdd:TIGR01135 222 IYNFE---GAPVQREVRVIDWDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIE-ENGGVFEELGAEEL--LKNIDRIQ 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 402 MIACGTSYHSCLATRAIFEELSDIPVSVELASDFLDRKCPVFRDDVCVFVSQSGETADTMLALNYCLERGALTVGIVNSV 481
Cdd:TIGR01135 296 IVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVP 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 482 GSSISRVTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLSDDR-VSKIDRRIEIIQGLKLIPGQIKQVLKLEPRIKK 560
Cdd:TIGR01135 376 GSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLYLLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAE 455
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 561 LcATELKDQKSLLLLGRGYQFAAALEGALKIKEISYMHSEGVLAGELKHGVLALVDENLPIIAFGTRDSLFPKVVSSIEQ 640
Cdd:TIGR01135 456 L-AERYADKRNFLFLGRGLGYPIALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEE 534
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322745 641 VTARKGHPIIICNENDEvwaqKSKSIDLQTLEVPQTVDCLQGLINIIPLQLMSYWLAVNKGIDVDFPRNLAKSVTVE 717
Cdd:TIGR01135 535 VKARGARVIVFAPEDDE----TIASVADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-716 |
9.64e-145 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 437.15 E-value: 9.64e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 1 MCGIFGYCnylverSRGEIIDTLVDGLQRLEYRGYDSTGIA-IDGDEADSTFIYKQIGK----VSALKEEITKQNPNrdv 75
Cdd:PTZ00295 24 CCGIVGYL------GNEDASKILLEGIEILQNRGYDSCGIStISSGGELKTTKYASDGTtsdsIEILKEKLLDSHKN--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 76 tfvSHCGIAHTRWATHGRPEQVNCHPQrSDPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAklylHLYNTN 155
Cdd:PTZ00295 95 ---STIGIAHTRWATHGGKTDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIA----NLIGLE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 156 LQNGhdLDFHELTKLVLLELEGSYGLLCKSCHYPNEVIATRKGSPLLIGVKSEkklkvdfvdvefpeenagqpeiplksn 235
Cdd:PTZ00295 167 LDQG--EDFQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDD--------------------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 236 nksfglgpkkarefeagsqnanllpiaanefnlrhsqsraflsedgsptpvEFFVSSDAASVVKHTKKVLFLEDDDLAHI 315
Cdd:PTZ00295 218 ---------------------------------------------------SIYVASEPSAFAKYTNEYISLKDGEIAEL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 316 -YDG--ELhihrsrrevgaSMTRSIQTLEMELAQIMKGPYDHFMQKEIYEQPESTFNTM--RGRIDYENNKVILGGLKAW 390
Cdd:PTZ00295 247 sLENvnDL-----------YTQRRVEKIPEEVIEKSPEPYPHWTLKEIFEQPIALSRALnnGGRLSGYNNRVKLGGLDQY 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 391 LPVVRRARRLIMIACGTSYHSCLATRAIFEELSDI-PVSVELASDFLDRKCPvfRDDVCV-FVSQSGETADTMLALNYCL 468
Cdd:PTZ00295 316 LEELLNIKNLILVGCGTSYYAALFAASIMQKLKCFnTVQVIDASELTLYRLP--DEDAGViFISQSGETLDVVRALNLAD 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 469 ERGALTVGIVNSVGSSISRVTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLSD--DRVSKIDRRIEIIQGLKLIPG 546
Cdd:PTZ00295 394 ELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQnkEYSCSNYKCSSLINSLHRLPT 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 547 QIKQVLKLEPRIKKLCATELKDQKSLLLLGRGYQFAAALEGALKIKEISYMHSEGVLAGELKHGVLALVDE--NLPIIAF 624
Cdd:PTZ00295 474 YIGMTLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKekNTPVILI 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 625 GTRDSLFPKVVSSIEQVTARKGHPIIICNENDEVwaqksKSIDLQTLEVPQTvDCLQGLINIIPLQLMSYWLAVNKGIDV 704
Cdd:PTZ00295 554 ILDDEHKELMINAAEQVKARGAYIIVITDDEDLV-----KDFADEIILIPSN-GPLTALLAVIPLQLLAYEIAILRGINP 627
|
730
....*....|..
gi 6322745 705 DFPRNLAKSVTV 716
Cdd:PTZ00295 628 DKPRGLAKTVTV 639
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-315 |
1.52e-108 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 328.25 E-value: 1.52e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 2 CGIFGYCNYlversrGEIIDTLVDGLQRLEYRGYDSTGIAIDGDeaDSTFIYKQIGKVSALKEEITKQNPNrdvtfvSHC 81
Cdd:cd00714 1 CGIVGYIGK------REAVDILLEGLKRLEYRGYDSAGIAVIGD--GSLEVVKAVGKVANLEEKLAEKPLS------GHV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 82 GIAHTRWATHGRPEQVNCHPQRSDPeDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHLYNTNlqnghd 161
Cdd:cd00714 67 GIGHTRWATHGEPTDVNAHPHRSCD-GEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGG------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 162 LDFHELTKLVLLELEGSYGLLCKSCHYPNEVIATRKGSPLLIGVKSEkklkvdfvdvefpeenagqpeiplksnnksfgl 241
Cdd:cd00714 140 LDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGDG--------------------------------- 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322745 242 gpkkarefeagsqnanllpiaanefnlrhsqsraflsedgsptpvEFFVSSDAASVVKHTKKVLFLEDDDLAHI 315
Cdd:cd00714 187 ---------------------------------------------ENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
556-715 |
1.98e-63 |
|
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: 207.89 E-value: 1.98e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 556 PRIKKLcATELKDQKSLLLLGRGYQFAAALEGALKIKEISYMHSEGVLAGELKHGVLALVDENLPIIAFGTRDSLFPKVV 635
Cdd:cd05009 1 EDIKEL-AEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 636 SSIEQVTARKGHPIIICNENDEvwaqksKSIDLQTLEVPQTVDCLQGLINIIPLQLMSYWLAVNKGIDVDFPRNLAKSVT 715
Cdd:cd05009 80 SLIKEVKARGAKVIVITDDGDA------KDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
358-717 |
1.58e-62 |
|
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: 212.07 E-value: 1.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 358 KEIYEQPES---TFNTMRGRIDYennkvILGGLKAwlpvvRRARRLIMIACGTSYHSCLATRAIFEELSDIPVSVELASD 434
Cdd:COG2222 2 REIAQQPEAwrrALAALAAAIAA-----LLARLRA-----KPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 435 FLDRKCPVFRD-DVCVFVSQSGETADTMLALNYCLERGALTVGIVNSVGSSISRVTHCGVHINAGPEIGVASTKAYTSQY 513
Cdd:COG2222 72 LVVYPAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTML 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 514 IALVMFALSLSDDRvskidrriEIIQGLKLIPGQIKQVLKLEPRIKKLCAteLKDQKSLLLLGRGYQFAAALEGALKIKE 593
Cdd:COG2222 152 LALLALLAAWGGDD--------ALLAALDALPAALEAALAADWPAAALAA--LADAERVVFLGRGPLYGLAREAALKLKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 594 ISYMHSEGVLAGELKHGVLALVDENLPIIAFGTRDSLFPKVVSSIEQVTARKGHPIIICNENDEVWaqksksidlqTLEV 673
Cdd:COG2222 222 LSAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAI----------TLPA 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 6322745 674 PQTV-DCLQGLINIIPLQLMSYWLAVNKGIDVDFPRNLAKSVTVE 717
Cdd:COG2222 292 IPDLhDALDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
399-524 |
7.16e-58 |
|
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: 191.94 E-value: 7.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 399 RLIMIACGTSYHSCLATRAIFEELSDIPVSVELASDFLDRKCPVFRDDVCVFVSQSGETADTMLALNYCLERGALTVGIV 478
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 6322745 479 NSVGSSISRVTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLS 524
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-211 |
6.75e-53 |
|
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: 182.26 E-value: 6.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 2 CGIFGYCNYLVERSRGEIIDTlvDGLQRLEYRGYDSTGIAIDGDEADSTFIYKQIGKVSALKEeitkqnpnRDVTFVSHC 81
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLL--RGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDL--------LDEPLKSGV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 82 GIAHTRWATHGRPEQVNCHPQRSDPeDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHLyntnlqnGHD 161
Cdd:cd00352 71 ALGHVRLATNGLPSEANAQPFRSED-GRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERL-------GRE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6322745 162 LDFHELTKLVLLELEGSYGLLCKSCHyPNEVIATRKG---SPLLIGVKSEKKL 211
Cdd:cd00352 143 GGLFEAVEDALKRLDGPFAFALWDGK-PDRLFAARDRfgiRPLYYGITKDGGL 194
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
395-522 |
5.56e-38 |
|
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: 137.43 E-value: 5.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 395 RRARRLIMIACGTSYHSCLATRAIFEELSDIPVSVELASDFLDRKCP-VFRDDVCVFVSQSGETADTMLALNYCLERGAL 473
Cdd:pfam01380 3 AKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLAlVDEDDLVIAISYSGETKDLLAAAELAKARGAK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 6322745 474 TVGIVNSVGSSISRVTHCGVHINAGPEIGVASTKAYTSQYIALVMFALS 522
Cdd:pfam01380 83 IIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
565-700 |
4.81e-32 |
|
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: 120.87 E-value: 4.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 565 ELKDQKSLLLLGRGYQFAAALEGALKIKEISYMHSEGVLAGELKHGVLALVDENLPIIAFGTRDSLFPKvVSSIEQVTAR 644
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDL-LAAAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 6322745 645 KGHPIIICNENDEVWAQKSkSIDLQTLEVPQTvdcLQGLINIIPLQLMSYWLAVNK 700
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREA-DHVLYINAGPET---GVASTKSITAQLAALDALAVA 131
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-204 |
1.38e-19 |
|
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: 88.67 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 2 CGIFG-YCNYLVERSrgeiidtLVDGLQRLEYRGYDSTGIAI-DGDEadsTFIYKQIGKVS-ALKEEITKQNPnrdvtfv 78
Cdd:cd00715 1 CGVFGiYGAEDAARL-------TYLGLYALQHRGQESAGIATsDGKR---FHTHKGMGLVSdVFDEEKLRRLP------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 79 SHCGIAHTRWATHGRPEQVNCHPQRSD-PEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHlyntnlq 157
Cdd:cd00715 64 GNIAIGHVRYSTAGSSSLENAQPFVVNsPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIAR------- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6322745 158 NGHDLDFHELTKLVLLELEGSYGLLCKSchyPNEVIATR--KG-SPLLIG 204
Cdd:cd00715 137 SLAKDDLFEAIIDALERVKGAYSLVIMT---ADGLIAVRdpHGiRPLVLG 183
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-205 |
1.21e-18 |
|
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: 89.31 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 1 MCGIFGYCnylverSRGEIIDTLVDGLQRLEYRGYDSTGIAI-DGDeadSTFIYKQIGKVS-ALKEEITKQnpnrdvtFV 78
Cdd:COG0034 7 ECGVFGIY------GHEDVAQLTYYGLYALQHRGQESAGIATsDGG---RFHLHKGMGLVSdVFDEEDLER-------LK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 79 SHCGIAHTRWATHGRPEQVNCHP-QRSDPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHlyntnlq 157
Cdd:COG0034 71 GNIAIGHVRYSTTGSSSLENAQPfYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIAR------- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6322745 158 NGHDLDFHELTKLVLLELEGSYGLlckschypneVIATRKGsplLIGV 205
Cdd:COG0034 144 ELTKEDLEEAIKEALRRVKGAYSL----------VILTGDG---LIAA 178
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-212 |
4.07e-17 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 81.55 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 2 CGIFGYCNYLVERSRGEIIdtlVDGLQRLEYRG-YDSTGIAIDGDEADSTF-------IYKQIGkvsaLKEEITKQNPNR 73
Cdd:cd01907 1 CGIFGIMSKDGEPFVGALL---VEMLDAMQERGpGDGAGFALYGDPDAFVYssgkdmeVFKGVG----YPEDIARRYDLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 74 DvtFVSHCGIAHTRWATHGRPEQVNCHPqrsdpedqF-----VVVHNGIITNFRELKTLLINKGYKFESDTDTECIAkLY 148
Cdd:cd01907 74 E--YKGYHWIAHTRQPTNSAVWWYGAHP--------FsigdiAVVHNGEISNYGSNREYLERFGYKFETETDTEVIA-YY 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322745 149 LHL-----YNTNLQNGHDLDFHELTKLVLLELEGSYGLLckSCHYPNEVIATRKGSplLIGVKSEKKLK 212
Cdd:cd01907 143 LDLllrkgGLPLEYYKHIIRMPEEERELLLALRLTYRLA--DLDGPFTIIVGTPDG--FIVIRDRIKLR 207
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-182 |
1.83e-16 |
|
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: 82.37 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 2 CGIFGYcnYLVERSRGEIIdtlVDGLQRLEYRGYDSTGIAIDGDeaDSTFIYKQIGKVSalkeeiTKQNPNRDVTFVSHC 81
Cdd:TIGR01134 1 CGVVGI--YGQEEVAASLT---YYGLYALQHRGQESAGISVFDG--NRFRLHKGNGLVS------DVFNEEHLQRLKGNV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 82 GIAHTRWATHGRPEQVNCHP-QRSDPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHLYNTNlqngh 160
Cdd:TIGR01134 68 GIGHVRYSTAGSSGLENAQPfVVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESK----- 142
|
170 180
....*....|....*....|..
gi 6322745 161 dLDFHELTKLVLLELEGSYGLL 182
Cdd:TIGR01134 143 -DDLFDAVARVLERVRGAYALV 163
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
79-151 |
1.19e-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: 71.18 E-value: 1.19e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322745 79 SHCGIAHTRWATHGRPEQVNcHPQRSdPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHL 151
Cdd:pfam13522 10 GGVALGHVRLAIVDLPDAGN-QPMLS-RDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEW 80
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-150 |
3.03e-14 |
|
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: 72.59 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 2 CGIFGYCNYlveRSRGEIIDTLVDGLQRLEYRGYDSTGIAIDGdeadstfiykqigkvsalkeeitkqnpnrdvtfvsHC 81
Cdd:cd00712 1 CGIAGIIGL---DGASVDRATLERMLDALAHRGPDGSGIWIDE-----------------------------------GV 42
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322745 82 GIAHTRWA----THGRpeQvnchPQRSDpEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLH 150
Cdd:cd00712 43 ALGHRRLSiidlSGGA--Q----PMVSE-DGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEE 108
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-150 |
3.88e-14 |
|
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: 75.64 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 1 MCGIFGYCNYLVERSRgeiiDTLVDGLQRLEYRGYDSTGIAIDGdeadstfiykqigkvsalkeeitkqnpnrdvtfvsH 80
Cdd:COG0367 1 MCGIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGIWVDG-----------------------------------G 41
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322745 81 CGIAHTR-----WATHGRpeQvnchPqRSDPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLH 150
Cdd:COG0367 42 VALGHRRlsiidLSEGGH--Q----P-MVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEE 109
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-216 |
1.90e-13 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 73.14 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 2 CGIFGycnyLVERSRGEIIDTLVDGLQRLEYRGYDSTGIAI-DGDEADstfIYKQIGKVS-ALKEEITKqnpnrdvTFVS 79
Cdd:PRK05793 15 CGVFG----VFSKNNIDVASLTYYGLYALQHRGQESAGIAVsDGEKIK---VHKGMGLVSeVFSKEKLK-------GLKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 80 HCGIAHTRWATHGRPEQVNCHPQRSDPEDQFV-VVHNGIITNFRELKTLLINKGYKFESDTDTECIaklyLHLYNTNLQN 158
Cdd:PRK05793 81 NSAIGHVRYSTTGASDLDNAQPLVANYKLGSIaIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVI----LNLIARSAKK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322745 159 GhdldFHELTKLVLLELEGSYGLLCKSchyPNEVIATR--KG-SPLLIGvksekKLKVDFV 216
Cdd:PRK05793 157 G----LEKALVDAIQAIKGSYALVILT---EDKLIGVRdpHGiRPLCLG-----KLGDDYI 205
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
399-523 |
1.64e-12 |
|
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: 64.52 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 399 RLIMIACGTSYHSCLATRAIFEELSDIPVSVELASDFLDRKCPVFRDD-VCVFVSQSGETADTMLALNYCLERGALTVGI 477
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 6322745 478 VNSVGSSIsrVTHCGVHINAGPEIGVASTKaytsqYIALVMFALSL 523
Cdd:cd05710 81 TDDEDSPL--AKLADYVIVYGFEIDAVEEK-----YLLLYMLALRL 119
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
101-152 |
2.13e-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: 64.46 E-value: 2.13e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 6322745 101 PQRSDPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHLY 152
Cdd:pfam13537 15 PMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW 66
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-172 |
7.62e-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: 63.18 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 1 MCGIFGYCNYLVERSrGEIIDTLVDGL-QRLEYRGY------DSTGIAIDGDEADSTFIYKQIGKVSALKEEITKQNPnr 73
Cdd:cd01908 1 MCRLLGYSGAPIPLE-PLLIRPSHSLLvQSGGPREMkgtvhaDGWGIGWYEGKGGRPFRYRSPLPAWSDINLESLARP-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 74 dvtFVSHCGIAHTRWATHGRPEQVNCHPQRsdpEDQFVVVHNGIITNFRELKTLLINKG-YKFESDTDTECIAKLYLhly 152
Cdd:cd01908 78 ---IKSPLVLAHVRAATVGPVSLENCHPFT---RGRWLFAHNGQLDGFRLLRRRLLRLLpRLPVGTTDSELAFALLL--- 148
|
170 180
....*....|....*....|
gi 6322745 153 nTNLQNGHDLDFHELTKLVL 172
Cdd:cd01908 149 -SRLLERDPLDPAELLDAIL 167
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-182 |
3.41e-10 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 62.77 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 1 MCGIFG-YCNYLVERsrgeiidTLVDGLQRLEYRGYDSTGI-AIDGDEADSTfiyKQIGKVS-ALKEEITKQNPnrdvtf 77
Cdd:PLN02440 1 ECGVVGiFGDPEASR-------LCYLGLHALQHRGQEGAGIvTVDGNRLQSI---TGNGLVSdVFDESKLDQLP------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 78 vSHCGIAHTRWATHGRPEQVNCHP-QRSDPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIaklyLHLYNTNL 156
Cdd:PLN02440 65 -GDIAIGHVRYSTAGASSLKNVQPfVANYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVL----LHLIAISK 139
|
170 180
....*....|....*....|....*.
gi 6322745 157 qngHDLDFHELTKlVLLELEGSYGLL 182
Cdd:PLN02440 140 ---ARPFFSRIVD-ACEKLKGAYSMV 161
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
79-182 |
1.11e-08 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 56.51 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 79 SHCGIAHTRWATHGRPEQVNCHPQRSdpeDQFVVVHNGIITNFRELKTLL---INKGYKF--ESDTDTECIAKLYLHlyn 153
Cdd:COG0121 76 SRLVIAHVRKATVGPVSLENTHPFRG---GRWLFAHNGQLDGFDRLRRRLaeeLPDELYFqpVGTTDSELAFALLLS--- 149
|
90 100 110
....*....|....*....|....*....|.
gi 6322745 154 tNLQNGHDLDFHELTKLV--LLELEGSYGLL 182
Cdd:COG0121 150 -RLRDGGPDPAEALAEALreLAELARAPGRL 179
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
445-519 |
1.45e-08 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 56.72 E-value: 1.45e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322745 445 DDVCVFVSQSGETADTMLALNYCLERGALTVGIVNSVGSSISRVTHCGVHINAGPEIGVAST--KAYTSQYIALVMF 519
Cdd:PRK05441 132 KDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMI 208
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
445-519 |
2.72e-08 |
|
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: 55.61 E-value: 2.72e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322745 445 DDVCVFVSQSGETADTMLALNYCLERGALTVGIVNSVGSSISRVTHCGVHINAGPEIGVAST--KAYTSQYIALVMF 519
Cdd:cd05007 119 RDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAGTAQKLALNML 195
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-148 |
9.91e-08 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 55.11 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 1 MCGIFGYCNYLVERSRgeiIDTLVDGL-QRLEYRGYDSTGIAIDGDEADSTFIykqigkvsalkeeitkqnpnrdvtfvs 79
Cdd:PTZ00077 1 MCGILAIFNSKGERHE---LRRKALELsKRLRHRGPDWSGIIVLENSPGTYNI--------------------------- 50
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322745 80 hcgIAHTRWA----THGRpeqvncHPQRSDPEDqFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLY 148
Cdd:PTZ00077 51 ---LAHERLAivdlSDGK------QPLLDDDET-VALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLY 113
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
445-519 |
1.72e-07 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 53.56 E-value: 1.72e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322745 445 DDVCVFVSQSGETADTMLALNYCLERGALTVGIVNSVGSSISRVTHCGVHINAGPEIgVA-ST--KAYTSQYIALVMF 519
Cdd:COG2103 133 GDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEV-ITgSTrlKAGTAQKLVLNML 209
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-152 |
4.53e-07 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 52.99 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 1 MCGIFGYCNylVERSRGEIIDTLVDGLQRLEYRGYDSTGIaidgdeadstfiykqigkvsalkeeitkqnpnrdvtFVSH 80
Cdd:PRK09431 1 MCGIFGILD--IKTDADELRKKALEMSRLMRHRGPDWSGI------------------------------------YASD 42
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322745 81 CGI-AHTRWA----THGRpeQvnchpQRSDPEDQFVVVHNGIITNFRELKTLLINKgYKFESDTDTECIaklyLHLY 152
Cdd:PRK09431 43 NAIlGHERLSivdvNGGA--Q-----PLYNEDGTHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVI----LALY 107
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
111-152 |
9.37e-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: 9.37e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6322745 111 VVVHNGIITNFRELKTLLINKGYKFESDTDTECIaklyLHLY 152
Cdd:TIGR01536 69 VIVFNGEIYNHEELREELEAKGYTFQTDSDTEVI----LHLY 106
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
400-478 |
3.60e-06 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 45.44 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 400 LIMIACGTSYHSCLATRAIFEELSDIPVSVELASDFLD--RKCPVFRDDVCVFVSQSGETADTMLALNYCLERGALTVGI 477
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 6322745 478 V 478
Cdd:cd04795 81 T 81
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
444-543 |
8.53e-06 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 48.00 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 444 RDDVCVFVSQSGETADTMLALNYCLERGALTVGIVNSVGSSISRvtHCGVHINAGPEIGVASTKAYTSQYIALVMF---- 519
Cdd:COG1737 182 PGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAK--LADVVLYVPSEEPTLRSSAFSSRVAQLALIdala 259
|
90 100
....*....|....*....|....*..
gi 6322745 520 ---ALSLSDDRVSKIDRRIEIIQGLKL 543
Cdd:COG1737 260 aavAQRDGDKARERLERTEALLSELRE 286
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
394-518 |
2.78e-05 |
|
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: 44.53 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 394 VRRARRLIMIACGTSYHSC--LATRAI-----FEELSDIPVSVELASDfldrkcpVFRDDVCVFVSQSGETADTMLALNY 466
Cdd:cd05013 10 LAKARRIYIFGVGSSGLVAeyLAYKLLrlgkpVVLLSDPHLQLMSAAN-------LTPGDVVIAISFSGETKETVEAAEI 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6322745 467 CLERGALTVGIVNSVGSSISRVTHcgVHINAGPEIGVASTKAYTSQYIALVM 518
Cdd:cd05013 83 AKERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
445-519 |
1.37e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 44.30 E-value: 1.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322745 445 DDVCVFVSQSGETADTMLALNYCLERGALTVGIVNSVGSSISRVTHCGVHINAGPEIGVAST--KAYTSQYIALVMF 519
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
36-122 |
4.19e-04 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 42.70 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 36 DSTGIAIDGDEADSTFIYKQIGKVSALKEeITKQNPNRdvtfvSHCGIAHTRWATHGRPEQVNCHP-QRSDPEDQFVVVH 114
Cdd:pfam13230 34 DGWGIAFYEGRGARVFKDPQPSADSPIAE-LVRRYPIR-----SRNVIAHIRKATQGRVTLENTHPfMRELWGRYWIFAH 107
|
....*...
gi 6322745 115 NGIITNFR 122
Cdd:pfam13230 108 NGDLKGYA 115
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
398-518 |
6.99e-04 |
|
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.
Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 40.22 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 398 RRLIMIACGTSYH---------SCLATRAIF----EEL-SDIPVsvelasdfldrkcpVFRDDVCVFVSQSGETADTMLA 463
Cdd:cd05014 1 GKVVVTGVGKSGHiarkiaatlSSTGTPAFFlhptEALhGDLGM--------------VTPGDVVIAISNSGETDELLNL 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322745 464 LNYCLERGALTVGIVNSVGSSISRVTH----CGVHINAGPeIGVASTKAYTSQYI---ALVM 518
Cdd:cd05014 67 LPHLKRRGAPIIAITGNPNSTLAKLSDvvldLPVEEEACP-LGLAPTTSTTAMLAlgdALAV 127
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
444-522 |
9.81e-03 |
|
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: 38.80 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322745 444 RDDVCVFVSQSGETADTMLALNYCLERGALTVGIVNSVGSSISRvtHCGVHINAGPE-----IGVASTkayTSQYIALVM 518
Cdd:COG0794 91 PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLAR--AADVVLDLPVEreacpLNLAPT---TSTTATLAL 165
|
....*
gi 6322745 519 F-ALS 522
Cdd:COG0794 166 GdALA 170
|
|
| |
