|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-600 |
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: 892.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 1 MCGIIGYVGDaDETLSVLLDGLSNLEYRGYDSAGVAV-GGDGLRVEKRAGQLDALEAALHDATVSGPVGIAHTRWSTHGP 79
Cdd:COG0449 1 MCGIVGYIGK-RDAAPILLEGLKRLEYRGYDSAGIAVlDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 80 PTDDNAHPHTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGLAPEAAVRAAADRLDGSYA 159
Cdd:COG0449 80 PSDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 160 LAVVVAGT-DALFAVRHDSPLVLGVGEGESFVASDVPAFLQRTRDVVYLDDDEFVRLDADGWTVTDADGAAVEKEVRTVE 238
Cdd:COG0449 160 LAVISADEpDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 239 WEAEQTGKSGYDHYMLKEIHEQPVSLRQCISGRVDElDGRITVEELDDvgAPET------VQFVACGTSYHAALYGARLL 312
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDE-DGRVVLDELNL--AAEDlrnidrIYIVACGTSYHAGLVGKYLI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 313 -RAAGIPANAYYAHEYATAPAPVSGADLVVGVTQSGETADTLSALREAGGRGAETLALTNVVGSTAARESDHVVYIRAGP 391
Cdd:COG0449 317 eELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 392 EIGVAATKTFSSQLVGVNLLTARLA-GRGV---DRRRDLIDGLRGVPSDVQAVLD-GSTAAAVVEEFVDATAFFFLGRGL 466
Cdd:COG0449 397 EIGVASTKAFTTQLAALYLLALYLArARGTlsaEEEAELLEELRKLPEKIEEVLDlEEQIEELAEKYADARNALFLGRGI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 467 DYPVALEGALKFKEITYEHAEGFAAGELKHGPLALVTSNTPVFAVITGDgEAARKTLGNVKEVEARDAPVVVVTD-GAAE 545
Cdd:COG0449 477 NYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQD-ELYEKTLSNIQEVKARGGKVIAIADeGDEE 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1434753018 546 AGRYADHVLEIPRTDERLAPLLANVQLQLVAYHMAARLERAIDKPRNLAKSVTVE 600
Cdd:COG0449 556 VEELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-600 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 838.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 1 MCGIIGYVGDaDETLSVLLDGLSNLEYRGYDSAGVAV-GGDGLRVEKRAGQLDALEAALHDATVSGPVGIAHTRWSTHGP 79
Cdd:PRK00331 1 MCGIVGYVGQ-RNAAEILLEGLKRLEYRGYDSAGIAVlDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 80 PTDDNAHPHTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGLAPEAAVRAAADRLDGSYA 159
Cdd:PRK00331 80 PTERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 160 LAVVVAG-TDALFAVRHDSPLVLGVGEGESFVASDVPAFLQRTRDVVYLDDDEFVRLDADGWTVTDADGAAVEKEVRTVE 238
Cdd:PRK00331 160 LAVIDKDePDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 239 WEAEQTGKSGYDHYMLKEIHEQPVSLRQCISGRVDEL-DGRITVEELDDVgapETVQFVACGTSYHAALYGARLL-RAAG 316
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDELgEGELADEDLKKI---DRIYIVACGTSYHAGLVAKYLIeSLAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 317 IPANAYYAHEYATAPAPVSGADLVVGVTQSGETADTLSALREAGGRGAETLALTNVVGSTAARESDHVVYIRAGPEIGVA 396
Cdd:PRK00331 317 IPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 397 ATKTFSSQLVGVNLLTARLA-GRGV---DRRRDLIDGLRGVPSDVQAVLDG-STAAAVVEEFVDATAFFFLGRGLDYPVA 471
Cdd:PRK00331 397 STKAFTAQLAVLYLLALALAkARGTlsaEEEADLVHELRELPALIEQVLDLkEQIEELAEDFADARNALFLGRGVDYPVA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 472 LEGALKFKEITYEHAEGFAAGELKHGPLALVTSNTPVFAVITgDGEAARKTLGNVKEVEARDAPVVVVTDGAAEAGRYAD 551
Cdd:PRK00331 477 LEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAP-NDELYEKTKSNIQEVKARGARVIVIADEGDEVAEEAD 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1434753018 552 HVLEIPRTDERLAPLLANVQLQLVAYHMAARLERAIDKPRNLAKSVTVE 600
Cdd:PRK00331 556 DVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-600 |
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: 760.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 2 CGIIGYVGDaDETLSVLLDGLSNLEYRGYDSAGVAVGGDG-LRVEKRAGQLDALEAALHDATVSGPVGIAHTRWSTHGPP 80
Cdd:TIGR01135 1 CGIVGYIGQ-RDAVPILLEGLKRLEYRGYDSAGIAVVDEGkLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 81 TDDNAHPHTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGLAPEAAVRAAADRLDGSYAL 160
Cdd:TIGR01135 80 TDENAHPHTDEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 161 AVVVAGT-DALFAVRHDSPLVLGVGEGESFVASDVPAFLQRTRDVVYLDDDEFVRLDADGWTVTDADGAAVEKEVRTVEW 239
Cdd:TIGR01135 160 AVLHADHpETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 240 EAEQTGKSGYDHYMLKEIHEQPVSLRQCISGRVDelDGRITVEELDDVGAPETV---QFVACGTSYHAALYGARLL-RAA 315
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIE--ENGGVFEELGAEELLKNIdriQIVACGTSYHAGLVAKYLIeRLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 316 GIPANAYYAHEYATAPAPVSGADLVVGVTQSGETADTLSALREAGGRGAETLALTNVVGSTAARESDHVVYIRAGPEIGV 395
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 396 AATKTFSSQLVGVNLLTARLAG-RGV---DRRRDLIDGLRGVPSDVQAVLDG-STAAAVVEEFVDATAFFFLGRGLDYPV 470
Cdd:TIGR01135 398 ASTKAFTTQLTVLYLLALALAKaRGTlsaEEEAELVDALRRLPDLVEQVLLAdESIAELAERYADKRNFLFLGRGLGYPI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 471 ALEGALKFKEITYEHAEGFAAGELKHGPLALVTSNTPVFAVITgDGEAARKTLGNVKEVEARDAPVVVVTDGAAEAGR-Y 549
Cdd:TIGR01135 478 ALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAP-KDSLLEKTKSNVEEVKARGARVIVFAPEDDETIAsV 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1434753018 550 ADHVLEIPRTDERLAPLLANVQLQLVAYHMAARLERAIDKPRNLAKSVTVE 600
Cdd:TIGR01135 557 ADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-599 |
2.73e-159 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 470.27 E-value: 2.73e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 1 MCGIIGYVGDaDETLSVLLDGLSNLEYRGYDSAGVAV--GGDGLRVEKRAGQ------LDALEAALHDATVSGPVGIAHT 72
Cdd:PTZ00295 24 CCGIVGYLGN-EDASKILLEGIEILQNRGYDSCGISTisSGGELKTTKYASDgttsdsIEILKEKLLDSHKNSTIGIAHT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 73 RWSTHGPPTDDNAHPHTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGLAPEAAVRAAAD 152
Cdd:PTZ00295 103 RWATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKSAIS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 153 RLDGSYALAVVVAGT-DALFAVRHDSPLVLGVGEGESFVASDVPAFLQRTRDVVYLDDDEFVRLDADGwtVTDadgAAVE 231
Cdd:PTZ00295 183 RLQGTWGLCIIHKDNpDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLEN--VND---LYTQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 232 KEVRTVEWEAEQTGKSGYDHYMLKEIHEQPVSLRQCIS--GRVDELDGRITVEELD----DVGAPETVQFVACGTSYHAA 305
Cdd:PTZ00295 258 RRVEKIPEEVIEKSPEPYPHWTLKEIFEQPIALSRALNngGRLSGYNNRVKLGGLDqyleELLNIKNLILVGCGTSYYAA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 306 LYGARLLR------------AAGIpaNAY-YAHEYATapapvsgadlVVGVTQSGETADTLSALREAGGRGAETLALTNV 372
Cdd:PTZ00295 338 LFAASIMQklkcfntvqvidASEL--TLYrLPDEDAG----------VIFISQSGETLDVVRALNLADELNLPKISVVNT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 373 VGSTAARESDHVVYIRAGPEIGVAATKTFSSQLVGVNLLTARLA-GRGV----DRRRDLIDGLRGVPSDVQAVLDG--ST 445
Cdd:PTZ00295 406 VGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAqNKEYscsnYKCSSLINSLHRLPTYIGMTLKSceEQ 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 446 AAAVVEEFVDATAFFFLGRGLDYPVALEGALKFKEITYEHAEGFAAGELKHGPLALV--TSNTPVFAVITGDgEAARKTL 523
Cdd:PTZ00295 486 CKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIdkEKNTPVILIILDD-EHKELMI 564
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434753018 524 GNVKEVEARDAPVVVVTDGAAEAGRYADHVLEIPRTDErLAPLLANVQLQLVAYHMAARLERAIDKPRNLAKSVTV 599
Cdd:PTZ00295 565 NAAEQVKARGAYIIVITDDEDLVKDFADEIILIPSNGP-LTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-600 |
6.03e-145 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 434.95 E-value: 6.03e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 1 MCGIIGYVG-----DADETLSVLLDGLSNLEYRGYDSAGVAVGGDGL------RVEKRAGQLDALEAALH---------- 59
Cdd:PLN02981 1 MCGIFAYLNynvprERRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSlessspLVFREEGKIESLVRSVYeevaetdlnl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 60 DATVSGPVGIAHTRWSTHGPPTDDNAHPHT-DERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLI----- 133
Cdd:PLN02981 81 DLVFENHAGIAHTRWATHGPPAPRNSHPQSsGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAkfvfd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 134 -ARELRGGLAPEAAVRAAADRLDGSYALAVVVAG-TDALFAVRHDSPLVLGVGEG------------------------E 187
Cdd:PLN02981 161 kLNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHyPNELVACKRGSPLLLGVKELpeeknssavftsegfltknrdkpkE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 188 SFVASDVPAFLQRTRDVVYLDDDEFVRLDADGWTVTDADG------------AAVEKEVRTVEWEAEQTGKSGYDHYMLK 255
Cdd:PLN02981 241 FFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENekgrgggglsrpASVERALSTLEMEVEQIMKGNYDHYMQK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 256 EIHEQPVSLRQCISGRVDELDGRIT--------VEELDDVGAPETVQFVACGTSYHAALYGARLLRA-AGIPANAYYAHE 326
Cdd:PLN02981 321 EIHEQPESLTTTMRGRLIRGGSGKAkrvllgglKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEElSGVPVTMELASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 327 YATAPAPVSGADLVVGVTQSGETADTLSALREAGGRGAETLALTNVVGSTAARESDHVVYIRAGPEIGVAATKTFSSQLV 406
Cdd:PLN02981 401 LLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQIV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 407 GVNLLTARLAGRGV---DRRRDLIDGLRGVPSDVQAVLD-GSTAAAVVEEFVDATAFFFLGRGLDYPVALEGALKFKEIT 482
Cdd:PLN02981 481 AMTMLALALGEDSIssrSRREAIIDGLFDLPNKVREVLKlDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVKEVA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 483 YEHAEGFAAGELKHGPLALVTSNTPVFAVITGDGeAARKTLGNVKEVEARDAPVVVVTDGAAEAGRYA---DHVLEIPRT 559
Cdd:PLN02981 561 LMHSEGILAGEMKHGPLALVDETLPIIVIATRDA-CFSKQQSVIQQLRARKGRLIVICSKGDASSVCPsggCRVIEVPQV 639
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1434753018 560 DERLAPLLANVQLQLVAYHMAARLERAIDKPRNLAKSVTVE 600
Cdd:PLN02981 640 EDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-600 |
1.37e-127 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 390.01 E-value: 1.37e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 1 MCGIIGYVG-----DADETLSVLLDGLSNLEYRGYDSAGVAVGGdGLRVEKRAGQL------------------------ 51
Cdd:PTZ00394 1 MCGIFGYANhnvprTVEQILNVLLDGIQKVEYRGYDSAGLAIDA-NIGSEKEDGTAasaptprpcvvrsvgnisqlrekv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 52 --DALEAALH--DATVSGPVGIAHTRWSTHGPPTDDNAHPHTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTE 127
Cdd:PTZ00394 80 fsEAVAATLPpmDATTSHHVGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 128 VV----PHLIARElrGGLAPEAAVRAAADRLDGSYALAV-VVAGTDALFAVRHDSPLVLGVGEG---------------- 186
Cdd:PTZ00394 160 VIsvlsEYLYTRK--GIHNFADLALEVSRMVEGSYALLVkSVYFPGQLAASRKGSPLMVGIRRTddrgcvmklqtydltd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 187 -----ESFVASDVPAFLQRTRDVVYLDDDEFVRLDADGWTVTDADG---AAVEKEVRTVEWEAEQTGKSGYDHYMLKEIH 258
Cdd:PTZ00394 238 lsgplEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAErqrSIVKREVQHLDAKPEGLSKGNYPHFMLKEIY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 259 EQPVSLRQCISGRVDELDGRITVEELDD-----VGAPETVQFVACGTSYHAALyGARLL--RAAGIPANAYYAHEYATAP 331
Cdd:PTZ00394 318 EQPESVISSMHGRIDFSSGTVQLSGFTQqsiraILTSRRILFIACGTSLNSCL-AVRPLfeELVPLPISVENASDFLDRR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 332 APVSGADLVVGVTQSGETADTLSALREAGGRGAETLALTNVVGSTAARESDHVVYIRAGPEIGVAATKTFSSQLVGVNLL 411
Cdd:PTZ00394 397 PRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 412 TARLAGRGV---DRRRDLIDGLRGVPSDVQAVLD--GSTAAAVVEEFVDATAFFFLGRGLDYPVALEGALKFKEITYEHA 486
Cdd:PTZ00394 477 ALLLSSDSVrlqERRNEIIRGLAELPAAISECLKitHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 487 EGFAAGELKHGPLALVTSNTPVFAVITGDGEAARKTLGnVKEVEARDAPVVVV-TDGAAEAGRYADHVLEIPRTDERLAP 565
Cdd:PTZ00394 557 EGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSA-VQQVKARGGAVVVFaTEVDAELKAAASEIVLVPKTVDCLQC 635
|
650 660 670
....*....|....*....|....*....|....*
gi 1434753018 566 LLANVQLQLVAYHMAARLERAIDKPRNLAKSVTVE 600
Cdd:PTZ00394 636 VVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-215 |
1.62e-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: 324.79 E-value: 1.62e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 2 CGIIGYVGDaDETLSVLLDGLSNLEYRGYDSAGVAVGGDG-LRVEKRAGQLDALEAALHDATVSGPVGIAHTRWSTHGPP 80
Cdd:cd00714 1 CGIVGYIGK-REAVDILLEGLKRLEYRGYDSAGIAVIGDGsLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 81 TDDNAHPHTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGLAPEAAVRAAADRLDGSYAL 160
Cdd:cd00714 80 TDVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1434753018 161 AVVVAGT-DALFAVRHDSPLVLGVGEGESFVASDVPAFLQRTRDVVYLDDDEFVRL 215
Cdd:cd00714 160 AVISKDEpDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
254-600 |
4.25e-69 |
|
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: 227.09 E-value: 4.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 254 LKEIHEQPVSLRQCISGRVDELDgritvEELDDVGA--PETVQFVACGTSYHAALYGARLLRAA-GIPANAYYAHEYATA 330
Cdd:COG2222 1 AREIAQQPEAWRRALAALAAAIA-----ALLARLRAkpPRRVVLVGAGSSDHAAQAAAYLLERLlGIPVAALAPSELVVY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 331 PAPVSGA-DLVVGVTQSGETADTLSALREAGGRGAETLALTNVVGSTAARESDHVVYIRAGPEIGVAATKTFSSQLVGVN 409
Cdd:COG2222 76 PAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 410 LLTARLAGrgvdrRRDLIDGLRGVPSDVQAVLDGSTAAAVVEEFVDATAFFFLGRGLDYPVALEGALKFKEITYEHAEGF 489
Cdd:COG2222 156 ALLAAWGG-----DDALLAALDALPAALEAALAADWPAAALAALADAERVVFLGRGPLYGLAREAALKLKELSAGHAEAY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 490 AAGELKHGPLALVTSNTPVFAVITGDgEAARKTLGNVKEVEARDAPVVVVTDgaaeAGRYADHVLEIPRTDERLAPLLAN 569
Cdd:COG2222 231 SAAEFRHGPKSLVDPGTLVVVLASED-PTRELDLDLAAELRALGARVVAIGA----EDDAAITLPAIPDLHDALDPLLLL 305
|
330 340 350
....*....|....*....|....*....|.
gi 1434753018 570 VQLQLVAYHMAARLERAIDKPRNLAKSVTVE 600
Cdd:COG2222 306 VVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-213 |
4.10e-60 |
|
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: 199.21 E-value: 4.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 2 CGIIGYVG---DADETLSVLLDGLSNLEYRGYDSAGVAV-GGDGLRVEKRAGQLDALEAALHDATVSGPVGIAHTRWSTH 77
Cdd:cd00352 1 CGIFGIVGadgAASLLLLLLLRGLAALEHRGPDGAGIAVyDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 78 GPPTDDNAHPHTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGLaPEAAVRAAADRLDGS 157
Cdd:cd00352 81 GLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGG-LFEAVEDALKRLDGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1434753018 158 YALAVVVAGTDALFAVRH---DSPLVLGVGEGESFV-ASDVPAFLQRT-RDVVYLDDDEFV 213
Cdd:cd00352 160 FAFALWDGKPDRLFAARDrfgIRPLYYGITKDGGLVfASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
446-598 |
2.60e-56 |
|
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: 186.70 E-value: 2.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 446 AAAVVEEFVDATAFFFLGRGLDYPVALEGALKFKEITYEHAEGFAAGELKHGPLALVTSNTPVFAVITGDgEAARKTLGN 525
Cdd:cd05009 3 IKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPED-RLEEKLESL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1434753018 526 VKEVEARDAPVVVVTDgAAEAGRYADHVLEIPRTDERLAPLLANVQLQLVAYHMAARLERAIDKPRNLAKSVT 598
Cdd:cd05009 82 IKEVKARGAKVIVITD-DGDAKDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
293-416 |
2.06e-49 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 167.29 E-value: 2.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 293 VQFVACGTSYHAALYGARLL-RAAGIPANAYYAHEYATAPAPVSGADLVVGVTQSGETADTLSALREAGGRGAETLALTN 371
Cdd:cd05008 2 ILIVGCGTSYHAALVAKYLLeRLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITN 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1434753018 372 VVGSTAARESDHVVYIRAGPEIGVAATKTFSSQLVGVNLLTARLA 416
Cdd:cd05008 82 VVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-210 |
6.16e-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: 126.81 E-value: 6.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 2 CGIIGYVGdADETLSVLLDGLSNLEYRGYDSAGVAV-GGDGLRVEKRAGQL-DALEAAlHDATVSGPVGIAHTRWSTHGP 79
Cdd:cd00715 1 CGVFGIYG-AEDAARLTYLGLYALQHRGQESAGIATsDGKRFHTHKGMGLVsDVFDEE-KLRRLPGNIAIGHVRYSTAGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 80 PTDDNAHP---HTDeRGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGlAPEAAVRAAADRLDG 156
Cdd:cd00715 79 SSLENAQPfvvNSP-LGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAKD-DLFEAIIDALERVKG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1434753018 157 SYALAVVVAgtDALFAVRhDS----PLVLG-VGEGESFVASDVPAFLQ----RTRDV-----VYLDDD 210
Cdd:cd00715 157 AYSLVIMTA--DGLIAVR-DPhgirPLVLGkLEGDGYVVASESCALDIigaeFVRDVepgeiVVIDDD 221
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-214 |
1.22e-31 |
|
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: 128.22 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 1 MCGIIGYVGdADETLSVLLDGLSNLEYRGYDSAGVAVG-GDGLRVEKRAGQL-DAL-EAALhdATVSGPVGIAHTRWSTH 77
Cdd:COG0034 7 ECGVFGIYG-HEDVAQLTYYGLYALQHRGQESAGIATSdGGRFHLHKGMGLVsDVFdEEDL--ERLKGNIAIGHVRYSTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 78 GPPTDDNAHPHTDE--RGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGlAPEAAVRAAADRLD 155
Cdd:COG0034 84 GSSSLENAQPFYVNspFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTKE-DLEEAIKEALRRVK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1434753018 156 GSYALAVVVAGTdaLFAVRhDS----PLVLGVGEGESFVASDVPAFlqrtrDVVyldDDEFVR 214
Cdd:COG0034 163 GAYSLVILTGDG--LIAAR-DPngirPLVLGKLEDGYVVASESCAL-----DIL---GAEFVR 214
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-227 |
1.68e-29 |
|
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: 121.27 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 2 CGIIGYVGDADETLSVLLDGLSNLEYRGYDSAGVAV-GGDGLRVEKRAGQLDALEAALHDATVSGPVGIAHTRWSTHGPP 80
Cdd:TIGR01134 1 CGVVGIYGQEEVAASLTYYGLYALQHRGQESAGISVfDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 81 TDDNAHPHTDE--RGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGLAPEAAVRAAADRLDGSY 158
Cdd:TIGR01134 81 GLENAQPFVVNspYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRGAY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1434753018 159 ALavVVAGTDALFAVRhDS----PLVLGVGEGESFVASDVPAFlqrtrDVVyldDDEFVRLDADGWTVTDADG 227
Cdd:TIGR01134 161 AL--VLMTEDGLVAVR-DPhgirPLVLGRRGDGYVVASESCAL-----DIL---GAEFVRDVEPGEVVVIFDG 222
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
292-414 |
1.13e-27 |
|
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: 108.16 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 292 TVQFVACGTSYHAALYGAR-LLRAAGIPANAYYAHEYATAP-APVSGADLVVGVTQSGETADTLSALREAGGRGAETLAL 369
Cdd:pfam01380 7 RIFVIGRGTSYAIALELALkFEEIGYKVVEVELASELRHGVlALVDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAI 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1434753018 370 TNVVGSTAARESDHVVYIRAGPEIGVAATKTFSSQLVGVNLLTAR 414
Cdd:pfam01380 87 TDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-219 |
2.22e-25 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 109.74 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 2 CGIIG-YVGDADETLSVLLDGLSNLEYRGYDSAGVAVG-GDGLRVEKRAGQL-DALEAALHDaTVSGPVGIAHTRWSTHG 78
Cdd:PRK05793 15 CGVFGvFSKNNIDVASLTYYGLYALQHRGQESAGIAVSdGEKIKVHKGMGLVsEVFSKEKLK-GLKGNSAIGHVRYSTTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 79 PPTDDNAHP--HTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGLAPEAAVRAAAdrLDG 156
Cdd:PRK05793 94 ASDLDNAQPlvANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKGLEKALVDAIQA--IKG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 157 SYALavVVAGTDALFAVRHDS---PLVLGVGEGESFVASDVPAF----LQRTRDVvylDDDEFVRLDADG 219
Cdd:PRK05793 172 SYAL--VILTEDKLIGVRDPHgirPLCLGKLGDDYILSSESCALdtigAEFIRDV---EPGEIVIIDEDG 236
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-213 |
1.02e-24 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 107.84 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 1 MCGIIGYVGDADETlSVLLDGLSNLEYRGYDSAG-VAVGGDGLRVEKRAGQLDALEAALHDATVSGPVGIAHTRWSTHGP 79
Cdd:PLN02440 1 ECGVVGIFGDPEAS-RLCYLGLHALQHRGQEGAGiVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 80 PTDDNAHP-HTDER-GRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGLapEAAVRAAADRLDGS 157
Cdd:PLN02440 80 SSLKNVQPfVANYRfGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARPF--FSRIVDACEKLKGA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434753018 158 YALAVVVAgtDALFAVRHDS---PLVLGV-GEGESFVASDVPAF----LQRTRDV-----VYLDDDEFV 213
Cdd:PLN02440 158 YSMVFLTE--DKLVAVRDPHgfrPLVMGRrSNGAVVFASETCALdligATYEREVnpgevIVVDKDKGV 224
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
460-581 |
1.36e-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: 99.30 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 460 FFLGRGLDYPVALEGALKFKEITYEHAEGFAAGELKHGPLALVTSNTPVFAvITGDGEAARKTLgNVKEVEARDAPVVVV 539
Cdd:pfam01380 9 FVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIA-ISYSGETKDLLA-AAELAKARGAKIIAI 86
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1434753018 540 TDGAAEA-GRYADHVLEIPRTDERLAPLLANVQLQLVAYHMAA 581
Cdd:pfam01380 87 TDSPGSPlAREADHVLYINAGPETGVASTKSITAQLAALDALA 129
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
71-199 |
1.54e-23 |
|
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: 96.05 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 71 HTRWSTHGPPTDdnAHP-HTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARElrGGlapeaavRA 149
Cdd:pfam13537 1 HRRLSIIDLEGG--AQPmVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAE--WG-------ED 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1434753018 150 AADRLDGSYALAVVVAGTDALFAVRhDS----PLVLGVGEGESFV-ASDVPAFLQ 199
Cdd:pfam13537 70 CVDRLNGMFAFAIWDRRRQRLFLAR-DRfgikPLYYGRDDGGRLLfASELKALLA 123
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
63-193 |
1.10e-21 |
|
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: 90.83 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 63 VSGPVGIAHTRWSTHGPPtDDNAHPHTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARelrggla 142
Cdd:pfam13522 8 VEGGVALGHVRLAIVDLP-DAGNQPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEE------- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1434753018 143 peaAVRAAADRLDGSYALAVVVAGTDALFAVRHD---SPLVLGVGEGESFVASD 193
Cdd:pfam13522 80 ---WGEDCLERLRGMFAFAIWDRRRRTLFLARDRlgiKPLYYGILGGGFVFASE 130
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-198 |
4.60e-21 |
|
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: 91.85 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 2 CGIIGYVG--DADETLSVLLDGLSNLEYRGYDSAGVAVggdglrvekragqldaleaalhdatvSGPVGIAHTRWSTHGP 79
Cdd:cd00712 1 CGIAGIIGldGASVDRATLERMLDALAHRGPDGSGIWI--------------------------DEGVALGHRRLSIIDL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 80 ptDDNAHPHTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGLapeaavraaaDRLDGSYA 159
Cdd:cd00712 55 --SGGAQPMVSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEEWGEDCL----------ERLNGMFA 122
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1434753018 160 LAVVVAGTDALFAVRhDS----PLVLGVGEGESFVASDVPAFL 198
Cdd:cd00712 123 FALWDKRKRRLFLAR-DRfgikPLYYGRDGGGLAFASELKALL 164
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-199 |
5.59e-20 |
|
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: 93.75 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 1 MCGIIGYVG-DADETLSVLLDGLSNLEYRGYDSAGVAvggdglrvekragqldaleaalhdatVSGPVGIAHTRWSTHGP 79
Cdd:COG0367 1 MCGIAGIIDfDGGADREVLERMLDALAHRGPDGSGIW--------------------------VDGGVALGHRRLSIIDL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 80 ptDDNAH-PHTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGLapeaavraaaDRLDGSY 158
Cdd:COG0367 55 --SEGGHqPMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEEWGEDCL----------ERLNGMF 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1434753018 159 ALAVVVAGTDALFAVRhDS----PLVLGVGEGESFVASDVPAFLQ 199
Cdd:COG0367 123 AFAIWDRRERRLFLAR-DRfgikPLYYAEDGGGLAFASELKALLA 166
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-196 |
8.03e-18 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 83.47 E-value: 8.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 2 CGIIG--------YVGdadetlSVLLDGLSNLEYRG-YDSAGVAV-GGDGLRVEKRAGQLDALEAALHDATV-------- 63
Cdd:cd01907 1 CGIFGimskdgepFVG------ALLVEMLDAMQERGpGDGAGFALyGDPDAFVYSSGKDMEVFKGVGYPEDIarrydlee 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 64 -SGPVGIAHTRWSTHGPPTDDNAHPHTDerGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELR-GGL 141
Cdd:cd01907 75 yKGYHWIAHTRQPTNSAVWWYGAHPFSI--GDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRkGGL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434753018 142 APEAAVRAAAD------------------RLDGSYalAVVVAGTDALFAVRHDS---PLVLGVGEGESFVASDVPA 196
Cdd:cd01907 153 PLEYYKHIIRMpeeerelllalrltyrlaDLDGPF--TIIVGTPDGFIVIRDRIklrPAVVAETDDYVAIASEECA 226
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
291-428 |
2.44e-17 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 82.67 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 291 ETVQFVACGTSYHAALYGARLLRAAGIPANAYY--AHEYATAPAPVSGADLVVGVTQSGETADTLSALREAGGRGAETLA 368
Cdd:COG1737 135 RRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDgdGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIA 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1434753018 369 LTNVVGSTAARESDHVVYIRA-GPEIGVAATKTFSSQLVGVNLLTARLAGRGVDRRRDLID 428
Cdd:COG1737 215 ITDSPLSPLAKLADVVLYVPSeEPTLRSSAFSSRVAQLALIDALAAAVAQRDGDKARERLE 275
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
291-411 |
5.68e-16 |
|
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: 74.96 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 291 ETVQFVACGTSYHAALYGARLLRAAGIPANAYY-AHEYATAPAPVSGADLVVGVTQSGETADTLSALREAGGRGAETLAL 369
Cdd:cd05013 14 RRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSdPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAI 93
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1434753018 370 TNVVGSTAARESDHVVYIRAGPE-IGVAATKTFSSQLVGVNLL 411
Cdd:cd05013 94 TDSANSPLAKLADIVLLVSSEEGdFRSSAFSSRIAQLALIDAL 136
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
3-222 |
1.84e-11 |
|
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: 66.59 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 3 GIIGYVGDADETLSVLLDGLSNLEYRGYDSAGVAVGGDGlrvekragqldaleaalhdatvsgpVGIAHTRWSTHGPptD 82
Cdd:TIGR01536 3 GFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIEYKDGN-------------------------AILGHRRLAIIDL--S 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 83 DNAHPHTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIareLRGGlapeaavRAAADRLDGSYALAV 162
Cdd:TIGR01536 56 GGAQPMSNEGKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLY---EEWG-------EECVDRLDGMFAFAL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434753018 163 VVAGTDALFAVRhD----SPLVLGVGEGESFVASDVPAFLQ-----RTRDVVYLDDDEFVRLDADGWTV 222
Cdd:TIGR01536 126 WDSEKGELFLAR-DrfgiKPLYYAYDGGQLYFASEIKALLAhpnikPFPDGAALAPGFGFVRVPPPSTF 193
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-196 |
7.56e-11 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 64.74 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 1 MCGIIGY---VGDADETLSVLLDGLSNLEYRGYDSAGVAVggdglrvekragqldaLEAALHDATVsgpvgIAHTRWSTH 77
Cdd:PTZ00077 1 MCGILAIfnsKGERHELRRKALELSKRLRHRGPDWSGIIV----------------LENSPGTYNI-----LAHERLAIV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 78 GPptDDNAHPHTDERGRVAVVHNGIIENYRELRDELERAGVTFASETDTEVVPHLIARELRGGLapeaavraaADRLDGS 157
Cdd:PTZ00077 60 DL--SDGKQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPKDF---------WNHLDGM 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1434753018 158 YALAVVVAGTDALFAVRhDS----PLVLGVGE-GESFVASDVPA 196
Cdd:PTZ00077 129 FATVIYDMKTNTFFAAR-DHigiiPLYIGYAKdGSIWFSSELKA 171
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-192 |
8.71e-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: 62.79 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 1 MCGIIGYVGDADETLSVLLDGLSNL--------EYRGY---DSAGVA---VGGDGLRVEKRAGQLDALEAALHDAT-VSG 65
Cdd:cd01908 1 MCRLLGYSGAPIPLEPLLIRPSHSLlvqsggprEMKGTvhaDGWGIGwyeGKGGRPFRYRSPLPAWSDINLESLARpIKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 66 PVGIAHTRWSTHGPPTDDNAHPHTdeRGRVAVVHNGIIENYRELRDELERAGVTF-ASETDTEVVPHLIARELRGGlape 144
Cdd:cd01908 81 PLVLAHVRAATVGPVSLENCHPFT--RGRWLFAHNGQLDGFRLLRRRLLRLLPRLpVGTTDSELAFALLLSRLLER---- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1434753018 145 aavraaaDRLDGSYALAVVVAGTDALFAVRHDSPLVLGVGEGESFVAS 192
Cdd:cd01908 155 -------DPLDPAELLDAILQTLRELAALAPPGRLNLLLSDGEYLIAT 195
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-225 |
2.66e-09 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 59.92 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 1 MCGIIGYVG---DADETLSVLLDGLSNLEYRGYDSAGVAVGGDGLrvekragqldaleaalhdatvsgpvgIAHTRWSTH 77
Cdd:PRK09431 1 MCGIFGILDiktDADELRKKALEMSRLMRHRGPDWSGIYASDNAI--------------------------LGHERLSIV 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 78 GPptDDNAHPHTDERGRVAVVHNGIIENYRELRDELERaGVTFASETDTEVVPHLIaRELrgGLapeaavrAAADRLDGS 157
Cdd:PRK09431 55 DV--NGGAQPLYNEDGTHVLAVNGEIYNHQELRAELGD-KYAFQTGSDCEVILALY-QEK--GP-------DFLDDLDGM 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 158 YALAVVVAGTDALFAVRhDS----PLVLGV-GEGESFVASDVPAFLQRTRDVV------YLD--DDEFVRLDADGWTVTD 224
Cdd:PRK09431 122 FAFALYDSEKDAYLIAR-DPigiiPLYYGYdEHGNLYFASEMKALVPVCKTIKefppghYYWskDGEFVRYYQRDWFDYD 200
|
.
gi 1434753018 225 A 225
Cdd:PRK09431 201 A 201
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
2-140 |
9.91e-09 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 56.51 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 2 CGIIGYVGDADETLS-VLLDGLSNLEYRGYDSA--------GVA--VGGDGLRVEKRAgqldalEAALHDAT-------V 63
Cdd:COG0121 1 CRLLGYSGNVPTDLEfLLLDPEHSLVRQSGATRegphadgwGIGwyEGDGEPRLYRDP------LPAWSDPNlrllarpI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 64 SGPVGIAHTRWSTHGPPTDDNAHPHTDerGRVAVVHNGIIENYRELRDELERAGVTFA-----SETDTEVVPHLIARELR 138
Cdd:COG0121 75 KSRLVIAHVRKATVGPVSLENTHPFRG--GRWLFAHNGQLDGFDRLRRRLAEELPDELyfqpvGTTDSELAFALLLSRLR 152
|
..
gi 1434753018 139 GG 140
Cdd:COG0121 153 DG 154
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
334-393 |
4.14e-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: 54.45 E-value: 4.14e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 334 VSGADLVVGVTQSGETADTLSALREAGGRGAETLALTNVVGSTAARESDHVVYIRAGPEI 393
Cdd:cd05007 116 LTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEV 175
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-196 |
7.94e-08 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 55.16 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 1 MCGIIGYVG--DADETLSVLLDGLS-NLEYRGYDSAGVAVGGDglrvekragqldaleaalhdatvsgpVGIAHTRWSTH 77
Cdd:PLN02549 1 MCGILAVLGcsDDSQAKRSRVLELSrRLRHRGPDWSGLYGNED--------------------------CYLAHERLAIM 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 78 GPPTDDnaHPHTDERGRVAVVHNGIIENYRELRDELERagVTFASETDTEVVPHLIarELRGglapeaavRAAADRLDGS 157
Cdd:PLN02549 55 DPESGD--QPLYNEDKTIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHLY--EEHG--------EEFVDMLDGM 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1434753018 158 YALAVVVAGTDALFAVRhD----SPLVLGVGEGES-FVASDVPA 196
Cdd:PLN02549 121 FSFVLLDTRDNSFIAAR-DhigiTPLYIGWGLDGSvWFASEMKA 163
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
293-390 |
1.01e-07 |
|
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: 50.65 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 293 VQFVACGTSYhAALYGA--RLLRAAGIPANAYYAHEYATA-PAPVSGADLVVGVTQSGETADTLSALREAGGRGAETLAL 369
Cdd:cd05710 2 VFFVGCGGSL-ADMYPAkyFLKKESKLPVFVYNAAEFLHTgPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90 100
....*....|....*....|.
gi 1434753018 370 TNVVGSTAARESDHVVYIRAG 390
Cdd:cd05710 81 TDDEDSPLAKLADYVIVYGFE 101
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
334-393 |
1.08e-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: 53.94 E-value: 1.08e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 334 VSGADLVVGVTQSGETADTLSALREAGGRGAETLALTNVVGSTAARESDHVVYIRAGPEI 393
Cdd:COG2103 130 LGPGDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEV 189
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
334-393 |
2.63e-07 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 52.48 E-value: 2.63e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 334 VSGADLVVGVTQSGETADTLSALREAGGRGAETLALTNVVGSTAARESDHVVYIRAGPEI 393
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEV 188
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
293-406 |
3.23e-07 |
|
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: 49.46 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 293 VQFVACGTSYHAALYGARLLRAAGIPAnaYYAHeyataPAP--------VSGADLVVGVTQSGETADTLSALREAGGRGA 364
Cdd:cd05014 3 VVVTGVGKSGHIARKIAATLSSTGTPA--FFLH-----PTEalhgdlgmVTPGDVVIAISNSGETDELLNLLPHLKRRGA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1434753018 365 ETLALTNVVGSTAARESDHVVYIRAGPE---IGVAATKTFSSQLV 406
Cdd:cd05014 76 PIIAITGNPNSTLAKLSDVVLDLPVEEEacpLGLAPTTSTTAMLA 120
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
299-370 |
5.61e-06 |
|
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: 45.72 E-value: 5.61e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1434753018 299 GTSYHAALYGARLLRA-AGIPAnayYAHEYATAPAPVSGADLVVGVTQSGETADTLSALREAGGRGAETLALT 370
Cdd:cd05017 8 GGSGIGGDLLESLLLDeAKIPV---YVVKDYTLPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAIT 77
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
316-385 |
5.85e-06 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 48.22 E-value: 5.85e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1434753018 316 GIPANAYY-AHEYATAPAPVSGADLVVGVTQSGETADTLSALREAGGRGAETLALTNVVGSTAARESDHVV 385
Cdd:PRK11337 166 GVRCQAYDdAHIMLMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
291-591 |
1.75e-05 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 47.30 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 291 ETVQFVACGTSYHAALYGARLL-RAAGIPANAYYAHEYA-TAPAPVSGADLVVGVTQSGETADTLSALREAGGRGAETLA 368
Cdd:PRK11382 45 DRIYFVACGSPLNAAQTAKHLAdRFSDLQVYAISGWEFCdNTPYRLDDRCAVIGVSDYGKTEEVIKALELGRACGALTAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 369 LTNVVGSTAARESDHVVYIRAGPEIGVAATKTFSsqlVGVNLLTARLAGRGVDRRRDlidGLRGVPSDVQAVLDG--STA 446
Cdd:PRK11382 125 FTKRADSPITSAAEFSIDYQADCIWEIHLLLCYS---VVLEMITRLAPNAEIGKIKN---DLKQLPNALGHLVRTweEKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 447 AAVVEEFVDATAFFFLGRGLDYPVAL-EGALKFKEITYEHAEGFAAGELKHGPLALVTSNTPvFAVITGDGEAARKTLGN 525
Cdd:PRK11382 199 RQLGELASQWPMIYTVAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVP-FLFLLGNDESRHTTERA 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434753018 526 VKEVEARDAPVVVVTDGAAEAGRYAdhvleiprtdeRLAPLLANVQLQLVAYHMAARLERAIDKPR 591
Cdd:PRK11382 278 INFVKQRTDNVIVIDYAEISQGLHP-----------WLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
293-370 |
2.45e-04 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 40.05 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 293 VQFVACGTSYHAALYGA-RLLRAAGIPANAYYAHEYATAPAPVSGA--DLVVGVTQSGETADTLSALREAGGRGAETLAL 369
Cdd:cd04795 1 IFVIGIGGSGAIAAYFAlELLELTGIEVVALIATELEHASLLSLLRkgDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 1434753018 370 T 370
Cdd:cd04795 81 T 81
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
331-370 |
3.37e-04 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 43.05 E-value: 3.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1434753018 331 PAPVSGADLVVGVTQSGETADTLSALREAGGRGAETLALT 370
Cdd:PRK08674 73 PAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKIIAIT 112
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
436-593 |
6.32e-04 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 42.22 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 436 DVQAVLDGSTAAAVVEEFVDATAFFFLGRGLDYPVALEGALKF----KEITYEHAEGFAAGELkhgpLALVTSNTPVFAV 511
Cdd:COG1737 114 ETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLlrlgKNVVLLDGDGHLQAES----AALLGPGDVVIAI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 512 -ITGdgeAARKTLGNVKEVEARDAPVVVVTD-GAAEAGRYADHVLEIPRTDE---------RLAPL-LANVQLQLVAYHM 579
Cdd:COG1737 190 sFSG---YTRETLEAARLAKERGAKVIAITDsPLSPLAKLADVVLYVPSEEPtlrssafssRVAQLaLIDALAAAVAQRD 266
|
170
....*....|....
gi 1434753018 580 AARLERAIDKPRNL 593
Cdd:COG1737 267 GDKARERLERTEAL 280
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
460-544 |
1.95e-03 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 37.74 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 460 FFLGRGLDYPVALEGALKFKEITYEHAEGFAAGELKHGPLALVTSNTPVFAVITGDGEAARKTLGnVKEVEARDAPVVVV 539
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLLRKGDVVIALSYSGRTEELLAA-LEIAKELGIPVIAI 80
|
....*
gi 1434753018 540 TDGAA 544
Cdd:cd04795 81 TDALA 85
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
461-590 |
2.75e-03 |
|
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: 38.76 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434753018 461 FLGRGLDYPVALEGALKFKEIT-------YEHAEGFaagelKHGPLALVTSNTPVFAVITGDGEAARKTLGNVKEVEaRD 533
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLELTagkvatvYDSPLGF-----RHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLLKELR-RD 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1434753018 534 AP---VVVVTDGA-AEAGRYADHVLEIPRT--DERLAPlLANVQLQLVAYHMAARLERAIDKP 590
Cdd:cd05010 77 GIaarVIAISPESdAGIEDNSHYYLPGSRDldDVYLAF-PYILYAQLFALFNSIALGLTPDNP 138
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
329-387 |
3.11e-03 |
|
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.
Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 39.10 E-value: 3.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1434753018 329 TAPAPVSGaDLVVGVTQSGETADTLSALREAGGRGAETLALTNVVGSTAARESDHVVYI 387
Cdd:cd05005 69 TTPAIGPG-DLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVI 126
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
338-412 |
3.80e-03 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 39.67 E-value: 3.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1434753018 338 DLVVGVTQSGETADTLSALREAGGRGAETLALTNVVGSTAARESDHVVYIRAGPEIGVAAT--KTFSSQLVGVNLLT 412
Cdd:PRK12570 129 DVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNMLS 205
|
|
| |
