|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-601 |
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: 862.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 1 MCGIIGCAGHEgDTVPVLLNGLARLEYRGYDSTGLAV-SNSDIHVVKREGELDELVETVESEiEVDGVAGVGHTRWSTHG 79
Cdd:COG0449 1 MCGIVGYIGKR-DAAPILLEGLKRLEYRGYDSAGIAVlDDGGLEVRKAVGKLANLEEKLAEE-PLSGTIGIGHTRWATHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 80 KPSDANAHPHTDCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVGHYLDAGSSPKAAFHRAVEKLEGSY 159
Cdd:COG0449 79 APSDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 160 AIAAVFESRKEVM-ATRQDSSLVLGVGDEATYVASDMTALIERTDSVIHLDDGEFAFLSPDGYTIIDEDGERQSKAQTTI 238
Cdd:COG0449 159 ALAVISADEPDRIvAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 239 EWDVEEITKGHHDHYMIKEIYEQSAALRECLRNRSTTDRLISLDTF----DDYHSVDRVHLVACGTSYHAALFGAQMLRE 314
Cdd:COG0449 239 DWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVVLDELnlaaEDLRNIDRIYIVACGTSYHAGLVGKYLIEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 315 -RGVSAQAFLASEYAMTPAPVQDGTLVVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEALYIRSGPEI 393
Cdd:COG0449 319 lARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 394 SVAATKTFASQLVTLTLFALHSS---STESNHETRRLVSALDELPGQIQRLFDTT-TAGEIASRLADGSGYFFIGRGLQY 469
Cdd:COG0449 399 GVASTKAFTTQLAALYLLALYLArarGTLSAEEEAELLEELRKLPEKIEEVLDLEeQIEELAEKYADARNALFLGRGINY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 470 PVALEGALKMKEITYEHAEGFAAGELKHGPLALVTDETPVFVSAVGDnETVRKTVANAEEVKARGAPLVAITD-GTSSIE 548
Cdd:COG0449 479 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQD-ELYEKTLSNIQEVKARGGKVIAIADeGDEEVE 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2339760666 549 RLADEVLRVPSTSRELAPVLVNVQYQLLAYHTARHLGRKIDKPRNLAKSVTVE 601
Cdd:COG0449 558 ELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-601 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 801.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 1 MCGIIGCAGHEgDTVPVLLNGLARLEYRGYDSTGLAV-SNSDIHVVKREGELDELVETVESEiEVDGVAGVGHTRWSTHG 79
Cdd:PRK00331 1 MCGIVGYVGQR-NAAEILLEGLKRLEYRGYDSAGIAVlDDGGLEVRKAVGKVANLEAKLEEE-PLPGTTGIGHTRWATHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 80 KPSDANAHPHTDCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVGHYLDAGSSPKAAFHRAVEKLEGSY 159
Cdd:PRK00331 79 KPTERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 160 AIAAVFESRKEVM-ATRQDSSLVLGVGDEATYVASDMTALIERTDSVIHLDDGEFAFLSPDGYTIIDEDGERQSKAQTTI 238
Cdd:PRK00331 159 ALAVIDKDEPDTIvAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 239 EWDVEEITKGHHDHYMIKEIYEQSAALRECLRNRSTTDRLISLDTfDDYHSVDRVHLVACGTSYHAALFGAQMLrER--G 316
Cdd:PRK00331 239 DWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDELGEGELAD-EDLKKIDRIYIVACGTSYHAGLVAKYLI-ESlaG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 317 VSAQAFLASEYAMTPAPVQDGTLVVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEALYIRSGPEISVA 396
Cdd:PRK00331 317 IPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 397 ATKTFASQLVTLTLFALH---SSSTESNHETRRLVSALDELPGQIQRLFDTT-TAGEIASRLADGSGYFFIGRGLQYPVA 472
Cdd:PRK00331 397 STKAFTAQLAVLYLLALAlakARGTLSAEEEADLVHELRELPALIEQVLDLKeQIEELAEDFADARNALFLGRGVDYPVA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 473 LEGALKMKEITYEHAEGFAAGELKHGPLALVTDETPVFVSAVgDNETVRKTVANAEEVKARGAPLVAITDGTSSIERLAD 552
Cdd:PRK00331 477 LEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAP-NDELYEKTKSNIQEVKARGARVIVIADEGDEVAEEAD 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2339760666 553 EVLRVPSTSRELAPVLVNVQYQLLAYHTARHLGRKIDKPRNLAKSVTVE 601
Cdd:PRK00331 556 DVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-601 |
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: 722.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 2 CGIIGCAGhEGDTVPVLLNGLARLEYRGYDSTGLAVSNSD-IHVVKREGELDELVETVEsEIEVDGVAGVGHTRWSTHGK 80
Cdd:TIGR01135 1 CGIVGYIG-QRDAVPILLEGLKRLEYRGYDSAGIAVVDEGkLFVRKAVGKVAELANKLG-EKPLPGGVGIGHTRWATHGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 81 PSDANAHPHTDCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVGHYLDAGSSPKAAFHRAVEKLEGSYA 160
Cdd:TIGR01135 79 PTDENAHPHTDEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 161 IAAVFESRKE-VMATRQDSSLVLGVGDEATYVASDMTALIERTDSVIHLDDGEFAFLSPDGYTIIDEDGERQSKAQTTIE 239
Cdd:TIGR01135 159 LAVLHADHPEtLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVID 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 240 WDVEEITKGHHDHYMIKEIYEQSAALRECLRNRSTTDR--LISLDTFDDYHSVDRVHLVACGTSYHAALFGAQMLrER-- 315
Cdd:TIGR01135 239 WDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGgvFEELGAEELLKNIDRIQIVACGTSYHAGLVAKYLI-ERla 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 316 GVSAQAFLASEYAMTPAPVQDGTLVVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEALYIRSGPEISV 395
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 396 AATKTFASQLVTLTLFALHSSS---TESNHETRRLVSALDELPGQIQR-LFDTTTAGEIASRLADGSGYFFIGRGLQYPV 471
Cdd:TIGR01135 398 ASTKAFTTQLTVLYLLALALAKargTLSAEEEAELVDALRRLPDLVEQvLLADESIAELAERYADKRNFLFLGRGLGYPI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 472 ALEGALKMKEITYEHAEGFAAGELKHGPLALVTDETPVFVSAvGDNETVRKTVANAEEVKARGAPLVAITD-GTSSIERL 550
Cdd:TIGR01135 478 ALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIA-PKDSLLEKTKSNVEEVKARGARVIVFAPeDDETIASV 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2339760666 551 ADEVLRVPSTSRELAPVLVNVQYQLLAYHTARHLGRKIDKPRNLAKSVTVE 601
Cdd:TIGR01135 557 ADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-600 |
5.43e-162 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 477.59 E-value: 5.43e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 1 MCGIIGCAGHEgDTVPVLLNGLARLEYRGYDSTGLAVSNSD-----------------IHVVKREGELDELVETVeseie 63
Cdd:PTZ00295 24 CCGIVGYLGNE-DASKILLEGIEILQNRGYDSCGISTISSGgelkttkyasdgttsdsIEILKEKLLDSHKNSTI----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 64 vdgvaGVGHTRWSTHGKPSDANAHPHTDCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVGHYLDAGSS 143
Cdd:PTZ00295 98 -----GIAHTRWATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGED 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 144 PKAAFHRAVEKLEGSYAIAAVFESRKEVM-ATRQDSSLVLGVGDEATYVASDMTALIERTDSVIHLDDGEFAFLSPDGYt 222
Cdd:PTZ00295 173 FQEAVKSAISRLQGTWGLCIIHKDNPDSLiVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENV- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 223 iidEDGERQSKAQtTIEWDVEEITKGHHDHYMIKEIYEQSAALRECLRNR---STTDRLISLDTFDDYH----SVDRVHL 295
Cdd:PTZ00295 252 ---NDLYTQRRVE-KIPEEVIEKSPEPYPHWTLKEIFEQPIALSRALNNGgrlSGYNNRVKLGGLDQYLeellNIKNLIL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 296 VACGTSYHAALFGAQMLRERGV--SAQAFLASEYAMTPAPVQDGTlVVGVTQSGETADTLAALRAADERGARTLALTNVV 373
Cdd:PTZ00295 328 VGCGTSYYAALFAASIMQKLKCfnTVQVIDASELTLYRLPDEDAG-VIFISQSGETLDVVRALNLADELNLPKISVVNTV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 374 GSSAARECDEALYIRSGPEISVAATKTFASQLVTLTLFAL----HSSSTESNHETRRLVSALDELPGQIQRLFDTTTA-- 447
Cdd:PTZ00295 407 GSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALwfaqNKEYSCSNYKCSSLINSLHRLPTYIGMTLKSCEEqc 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 448 GEIASRLADGSGYFFIGRGLQYPVALEGALKMKEITYEHAEGFAAGELKHGPLALV--TDETPVfVSAVGDNETVRKTVA 525
Cdd:PTZ00295 487 KRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIdkEKNTPV-ILIILDDEHKELMIN 565
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2339760666 526 NAEEVKARGAPLVAITDGTSSIERLADEVLRVPSTSrELAPVLVNVQYQLLAYHTARHLGRKIDKPRNLAKSVTV 600
Cdd:PTZ00295 566 AAEQVKARGAYIIVITDDEDLVKDFADEIILIPSNG-PLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-601 |
1.23e-143 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 431.87 E-value: 1.23e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 1 MCGI-----IGCAGHEGDTVPVLLNGLARLEYRGYDSTGLAVSNSDIH------VVKREGELDELVETVESEIEVDGV-- 67
Cdd:PLN02981 1 MCGIfaylnYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLesssplVFREEGKIESLVRSVYEEVAETDLnl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 68 -------AGVGHTRWSTHGKPSDANAHPHT-DCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVGHYLD 139
Cdd:PLN02981 81 dlvfenhAGIAHTRWATHGPPAPRNSHPQSsGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 140 --AGSSPKAAFHRAV----EKLEGSYAIaaVFESR---KEVMATRQDSSLVLGV----GDEAT----------------- 189
Cdd:PLN02981 161 klNEEEGDVTFSQVVmevmRQLEGAYAL--IFKSPhypNELVACKRGSPLLLGVkelpEEKNSsavftsegfltknrdkp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 190 ---YVASDMTALIERTDSVIHLDDGEFAFLSPDGYTIIDEDGERQS------------KAQTTIEWDVEEITKGHHDHYM 254
Cdd:PLN02981 239 kefFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRgggglsrpasveRALSTLEMEVEQIMKGNYDHYM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 255 IKEIYEQSAALRECLRNR-----STTDRLISLDTFDDYHSV----DRVHLVACGTSYHAALFGAQMLRE-RGVSAQAFLA 324
Cdd:PLN02981 319 QKEIHEQPESLTTTMRGRlirggSGKAKRVLLGGLKDHLKTirrsRRIVFIGCGTSYNAALAARPILEElSGVPVTMELA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 325 SEYAMTPAPVQDGTLVVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEALYIRSGPEISVAATKTFASQ 404
Cdd:PLN02981 399 SDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 405 LVTLTLFALH-SSSTESNHETR-RLVSALDELPGQIQRLFDTTTA-GEIASRLADGSGYFFIGRGLQYPVALEGALKMKE 481
Cdd:PLN02981 479 IVAMTMLALAlGEDSISSRSRReAIIDGLFDLPNKVREVLKLDQEmKELAELLIDEQSLLVFGRGYNYATALEGALKVKE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 482 ITYEHAEGFAAGELKHGPLALVTDETPVFVSAVGDNeTVRKTVANAEEVKARGAPLVAIT---DGTSSIERLADEVLRVP 558
Cdd:PLN02981 559 VALMHSEGILAGEMKHGPLALVDETLPIIVIATRDA-CFSKQQSVIQQLRARKGRLIVICskgDASSVCPSGGCRVIEVP 637
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2339760666 559 STSRELAPVLVNVQYQLLAYHTARHLGRKIDKPRNLAKSVTVE 601
Cdd:PLN02981 638 QVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-601 |
4.20e-116 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 360.35 E-value: 4.20e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 1 MCGIIGCAGHE-----GDTVPVLLNGLARLEYRGYDSTGLAVSNSDIH----------------VVKREGELDELVETVE 59
Cdd:PTZ00394 1 MCGIFGYANHNvprtvEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSekedgtaasaptprpcVVRSVGNISQLREKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 60 SE----------IEVDGVAGVGHTRWSTHGKPSDANAHPHTDCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEV 129
Cdd:PTZ00394 81 SEavaatlppmdATTSHHVGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 130 IPHLVGH-YLDAGSSPKAAFHRAVEK-LEGSYA--IAAVFESrKEVMATRQDSSLVLGV--------------------- 184
Cdd:PTZ00394 161 ISVLSEYlYTRKGIHNFADLALEVSRmVEGSYAllVKSVYFP-GQLAASRKGSPLMVGIrrtddrgcvmklqtydltdls 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 185 GDEATYVASDMTALIERTDSVIHLDDGEFAFLSpDGYTIIDEDGERQ----SKAQTTIEWDVEEITKGHHDHYMIKEIYE 260
Cdd:PTZ00394 240 GPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYC-DGALRFYNAAERQrsivKREVQHLDAKPEGLSKGNYPHFMLKEIYE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 261 QSAALRECLRNR-STTDRLISLDTFDDYH-----SVDRVHLVACGTSYHAALfGAQMLRERGVSAQAFL--ASEYAMTPA 332
Cdd:PTZ00394 319 QPESVISSMHGRiDFSSGTVQLSGFTQQSirailTSRRILFIACGTSLNSCL-AVRPLFEELVPLPISVenASDFLDRRP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 333 PVQDGTLVVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEALYIRSGPEISVAATKTFASQLVTLTLFA 412
Cdd:PTZ00394 398 RIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 413 LHSSSTESNHETRRL--VSALDELPGQIQRLFDTT--TAGEIASRLADGSGYFFIGRGLQYPVALEGALKMKEITYEHAE 488
Cdd:PTZ00394 478 LLLSSDSVRLQERRNeiIRGLAELPAAISECLKIThdPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 489 GFAAGELKHGPLALVTDETPVFVSAVGDNETVRKTVAnAEEVKARGAPLVAI-TDGTSSIERLADEVLRVPSTSRELAPV 567
Cdd:PTZ00394 558 GIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSA-VQQVKARGGAVVVFaTEVDAELKAAASEIVLVPKTVDCLQCV 636
|
650 660 670
....*....|....*....|....*....|....
gi 2339760666 568 LVNVQYQLLAYHTARHLGRKIDKPRNLAKSVTVE 601
Cdd:PTZ00394 637 VNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-216 |
5.14e-104 |
|
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: 313.23 E-value: 5.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 2 CGIIGCAGHeGDTVPVLLNGLARLEYRGYDSTGLAV-SNSDIHVVKREGELDELVETVEsEIEVDGVAGVGHTRWSTHGK 80
Cdd:cd00714 1 CGIVGYIGK-REAVDILLEGLKRLEYRGYDSAGIAViGDGSLEVVKAVGKVANLEEKLA-EKPLSGHVGIGHTRWATHGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 81 PSDANAHPHTDCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVGHYLDAGSSPKAAFHRAVEKLEGSYA 160
Cdd:cd00714 79 PTDVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2339760666 161 IAAVFESRK-EVMATRQDSSLVLGVGDEATYVASDMTALIERTDSVIHLDDGEFAFL 216
Cdd:cd00714 159 LAVISKDEPdEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
256-601 |
6.83e-76 |
|
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: 244.81 E-value: 6.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 256 KEIYEQSAALRECL-RNRSTTDRLISLDTFDDYhsvDRVHLVACGTSYHAALFGAQMLRER-GVSAQAFLASEYAMTPAP 333
Cdd:COG2222 2 REIAQQPEAWRRALaALAAAIAALLARLRAKPP---RRVVLVGAGSSDHAAQAAAYLLERLlGIPVAALAPSELVVYPAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 334 VQD-GTLVVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEALYIRSGPEISVAATKTFASQLVTLTLFA 412
Cdd:COG2222 79 LKLeGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 413 LHSSSTESnhetrrLVSALDELPGQIQRLFDTTTAGEIASRLADGSGYFFIGRGLQYPVALEGALKMKEITYEHAEGFAA 492
Cdd:COG2222 159 AAWGGDDA------LLAALDALPAALEAALAADWPAAALAALADAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 493 GELKHGPLALVTDETPVFVsAVGDNETVRKTVANAEEVKARGAPLVAITDGtssiERLADEVLRVPSTSRELAPVLVNVQ 572
Cdd:COG2222 233 AEFRHGPKSLVDPGTLVVV-LASEDPTRELDLDLAAELRALGARVVAIGAE----DDAAITLPAIPDLHDALDPLLLLVV 307
|
330 340
....*....|....*....|....*....
gi 2339760666 573 YQLLAYHTARHLGRKIDKPRNLAKSVTVE 601
Cdd:COG2222 308 AQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-214 |
2.92e-57 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 191.89 E-value: 2.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 2 CGIIGCAGHEGDTVPVLL---NGLARLEYRGYDSTGLAVSNSDIHVVKREGELDELVETVESEIEVDGVAGVGHTRWSTH 78
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 79 GKPSDANAHPHTDCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVGHYLDAGsSPKAAFHRAVEKLEGS 158
Cdd:cd00352 81 GLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREG-GLFEAVEDALKRLDGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2339760666 159 YAIAAVFESRKEVMATR---QDSSLVLGVG-DEATYVASDMTALIERT-DSVIHLDDGEFA 214
Cdd:cd00352 160 FAFALWDGKPDRLFAARdrfGIRPLYYGITkDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
449-599 |
4.06e-57 |
|
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: 189.01 E-value: 4.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 449 EIASRLADGSGYFFIGRGLQYPVALEGALKMKEITYEHAEGFAAGELKHGPLALVTDETPVFVSAVGDnETVRKTVANAE 528
Cdd:cd05009 5 ELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPED-RLEEKLESLIK 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2339760666 529 EVKARGAPLVAITDgTSSIERLADEVLRVPSTSRELAPVLVNVQYQLLAYHTARHLGRKIDKPRNLAKSVT 599
Cdd:cd05009 84 EVKARGAKVIVITD-DGDAKDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
292-414 |
1.52e-52 |
|
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: 175.76 E-value: 1.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 292 RVHLVACGTSYHAALFGAQMLRER-GVSAQAFLASEYAMTPAPVQDGTLVVGVTQSGETADTLAALRAADERGARTLALT 370
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLaGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2339760666 371 NVVGSSAARECDEALYIRSGPEISVAATKTFASQLVTLTLFALH 414
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALA 124
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-198 |
1.56e-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: 127.83 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 1 MCGIIGCAGHEgDTVPVLLNGLARLEYRGYDSTGLAVSN-SDIHVVKREGeldeLVETV--ESEIE-VDGVAGVGHTRWS 76
Cdd:COG0034 7 ECGVFGIYGHE-DVAQLTYYGLYALQHRGQESAGIATSDgGRFHLHKGMG----LVSDVfdEEDLErLKGNIAIGHVRYS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 77 THGKPSDANAHPHT-DCENR-VAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVGHYLDAGsSPKAAFHRAVEK 154
Cdd:COG0034 82 TTGSSSLENAQPFYvNSPFGsIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTKE-DLEEAIKEALRR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2339760666 155 LEGSYAIaaVFESRKEVMATRqDSS----LVLGVGDEATYVASDMTAL 198
Cdd:COG0034 161 VKGAYSL--VILTGDGLIAAR-DPNgirpLVLGKLEDGYVVASESCAL 205
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-198 |
3.32e-29 |
|
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: 116.41 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 2 CGIIGCAGHEgDTVPVLLNGLARLEYRGYDSTGLAVSNSD-IHVVKREGeldeLVETV--ESEIE-VDGVAGVGHTRWST 77
Cdd:cd00715 1 CGVFGIYGAE-DAARLTYLGLYALQHRGQESAGIATSDGKrFHTHKGMG----LVSDVfdEEKLRrLPGNIAIGHVRYST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 78 HGKPSDANAHP---HTdCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVGHYLDAGsSPKAAFHRAVEK 154
Cdd:cd00715 76 AGSSSLENAQPfvvNS-PLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAKD-DLFEAIIDALER 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2339760666 155 LEGSYAIAAVFesRKEVMATRqDSS----LVLG-VGDEATYVASDMTAL 198
Cdd:cd00715 154 VKGAYSLVIMT--ADGLIAVR-DPHgirpLVLGkLEGDGYVVASESCAL 199
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
287-413 |
4.81e-28 |
|
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: 108.93 E-value: 4.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 287 YHSVDRVHLVACGTSYHAALFGAQMLRERGVSAQAF-LASEYAMTP-APVQDGTLVVGVTQSGETADTLAALRAADERGA 364
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVeLASELRHGVlALVDEDDLVIAISYSGETKDLLAAAELAKARGA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2339760666 365 RTLALTNVVGSSAARECDEALYIRSGPEISVAATKTFASQLVTLTLFAL 413
Cdd:pfam01380 82 KIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAV 130
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-215 |
2.47e-26 |
|
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: 112.03 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 2 CGIIGCAGHEGDTVPVLLNGLARLEYRGYDSTGLAVSNSD-IHVVKREGELDElVETVESEIEVDGVAGVGHTRWSTHGK 80
Cdd:TIGR01134 1 CGVVGIYGQEEVAASLTYYGLYALQHRGQESAGISVFDGNrFRLHKGNGLVSD-VFNEEHLQRLKGNVGIGHVRYSTAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 81 PSDANAHPHT--DCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVGHYLDAGSSPKAAFHRAVEKLEGS 158
Cdd:TIGR01134 80 SGLENAQPFVvnSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRGA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 159 YAIAAVFESRkeVMATRqDS----SLVLGVGDEATYVASDMTAL------IERTDS---VIHLDDGEFAF 215
Cdd:TIGR01134 160 YALVLMTEDG--LVAVR-DPhgirPLVLGRRGDGYVVASESCALdilgaeFVRDVEpgeVVVIFDGGLES 226
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
461-581 |
7.21e-25 |
|
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: 100.07 E-value: 7.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 461 FFIGRGLQYPVALEGALKMKEITYEHAEGFAAGELKHGPLALVTDETPVFvsAVGDNETVRKTVANAEEVKARGAPLVAI 540
Cdd:pfam01380 9 FVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVI--AISYSGETKDLLAAAELAKARGAKIIAI 86
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2339760666 541 TD-GTSSIERLADEVLRVPSTSRELAPVLVNVQYQLLAYHTA 581
Cdd:pfam01380 87 TDsPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDAL 128
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-250 |
4.19e-21 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 96.64 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 2 CGIIGCAGHEGDTVPVLLN-GLARLEYRGYDSTGLAVSN-SDIHVVKREGeldeLVETVESEIEVD---GVAGVGHTRWS 76
Cdd:PRK05793 15 CGVFGVFSKNNIDVASLTYyGLYALQHRGQESAGIAVSDgEKIKVHKGMG----LVSEVFSKEKLKglkGNSAIGHVRYS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 77 THGKPSDANAHP---HTDCENrVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVGHYldAGSSPKAAFHRAVE 153
Cdd:PRK05793 91 TTGASDLDNAQPlvaNYKLGS-IAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARS--AKKGLEKALVDAIQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 154 KLEGSYAIAAVFEsrKEVMATRQDSS---LVLGVGDEATYVASDMTALiertDSVihldDGEFAF-LSPDGYTIIDEDGE 229
Cdd:PRK05793 168 AIKGSYALVILTE--DKLIGVRDPHGirpLCLGKLGDDYILSSESCAL----DTI----GAEFIRdVEPGEIVIIDEDGI 237
|
250 260
....*....|....*....|.
gi 2339760666 230 RQSKaqttiewdVEEITKGHH 250
Cdd:PRK05793 238 KSIK--------FAEKTKCQT 250
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-198 |
3.78e-20 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 93.59 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 1 MCGIIGCAGhEGDTVPVLLNGLARLEYRGYDSTGLAVSNSD-IHVVKREGeldeLVETVESE---IEVDGVAGVGHTRWS 76
Cdd:PLN02440 1 ECGVVGIFG-DPEASRLCYLGLHALQHRGQEGAGIVTVDGNrLQSITGNG----LVSDVFDEsklDQLPGDIAIGHVRYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 77 THGKPSDANAHP-HTDCE-NRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVghyldAGSSPKAAFHRAV-- 152
Cdd:PLN02440 76 TAGASSLKNVQPfVANYRfGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLI-----AISKARPFFSRIVda 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2339760666 153 -EKLEGSYAIAAVFESRkeVMATRQDSS---LVLGVGDEATYV-ASDMTAL 198
Cdd:PLN02440 151 cEKLKGAYSMVFLTEDK--LVAVRDPHGfrpLVMGRRSNGAVVfASETCAL 199
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
60-194 |
6.99e-20 |
|
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: 85.82 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 60 SEIEVDGVAGVGHTRWSTHGKPSDANaHPHTDCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLvghYLD 139
Cdd:pfam13522 4 SGIWVEGGVALGHVRLAIVDLPDAGN-QPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL---YEE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2339760666 140 AGsspkaafHRAVEKLEGSYAIAAVFESRKEVMATRQD---SSLVLGVGDEATYVASD 194
Cdd:pfam13522 80 WG-------EDCLERLRGMFAFAIWDRRRRTLFLARDRlgiKPLYYGILGGGFVFASE 130
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-200 |
1.06e-19 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 88.00 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 2 CGIIGCAGHEG--DTVPVLLNGLARLEYRGYDSTGlavsnsdihvvkregeldelvetveseIEVDGVAGVGHTRWSTHG 79
Cdd:cd00712 1 CGIAGIIGLDGasVDRATLERMLDALAHRGPDGSG---------------------------IWIDEGVALGHRRLSIID 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 80 KpsDANAHPHTDCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLvghYLDAGsspkaafHRAVEKLEGSY 159
Cdd:cd00712 54 L--SGGAQPMVSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL---YEEWG-------EDCLERLNGMF 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2339760666 160 AIAAVFESRKEVMATRqDS----SLVLGVGDEATYVASDMTALIE 200
Cdd:cd00712 122 AFALWDKRKRRLFLAR-DRfgikPLYYGRDGGGLAFASELKALLA 165
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-172 |
7.18e-17 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 83.73 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 1 MCGIIGCAG-HEGDTVPVLLNGLARLEYRGYDSTGlavsnsdihvvkregeldelvetveseIEVDGVAGVGHTRWSTHG 79
Cdd:COG0367 1 MCGIAGIIDfDGGADREVLERMLDALAHRGPDGSG---------------------------IWVDGGVALGHRRLSIID 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 80 kPSDANAHPHTDCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLvghYLDAGSSpkaafhrAVEKLEGSY 159
Cdd:COG0367 54 -LSEGGHQPMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA---YEEWGED-------CLERLNGMF 122
|
170
....*....|...
gi 2339760666 160 AIaAVFESRKEVM 172
Cdd:COG0367 123 AF-AIWDRRERRL 134
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
72-198 |
2.57e-16 |
|
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: 75.25 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 72 HTRWSTHGkpSDANAHP-HTDCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLV-GHYLDAgsspkaafh 149
Cdd:pfam13537 1 HRRLSIID--LEGGAQPmVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYeAEWGED--------- 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2339760666 150 rAVEKLEGSYAIAAVFESRKEVMATRqDS----SLVLGVGDEAT-YVASDMTAL 198
Cdd:pfam13537 70 -CVDRLNGMFAFAIWDRRRQRLFLAR-DRfgikPLYYGRDDGGRlLFASELKAL 121
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
95-363 |
6.16e-16 |
|
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: 80.46 E-value: 6.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 95 RVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLvghYLDAGSspkaafhRAVEKLEGSYAIaAVFESRKEVMAT 174
Cdd:TIGR01536 67 TYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHL---YEEWGE-------ECVDRLDGMFAF-ALWDSEKGELFL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 175 RQDSslvLGV-------GDEATYVASDMTALiertdsvihLDDGEFAFLsPDGYTIIDEDGERQSKAQTTIEWDVEEITK 247
Cdd:TIGR01536 136 ARDR---FGIkplyyayDGGQLYFASEIKAL---------LAHPNIKPF-PDGAALAPGFGFVRVPPPSTFFRGVFELEP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 248 GH----HDHYMIKEIYEQSAALRECLRNRSTTDRLISLDTfddyHSVDRvHLVAcgtsyhaalfgaqmLRERGV------ 317
Cdd:TIGR01536 203 GHdlplDDDGLNIERYYWERRDEHTDSEEDLVDELRSLLE----DAVKR-RLVA--------------DVPVGVllsggl 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2339760666 318 --SAQAFLASEYAmTPAPVQdgTLVVGVTQSGETADTLAALRAADERG 363
Cdd:TIGR01536 264 dsSLVAAIARREA-PRGPVH--TFSIGFEGSPDFDESKYARKVADHLG 308
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-198 |
4.21e-15 |
|
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: 75.38 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 2 CGIIGCA--GHEGDTVPVLLNGLARLEYRG-YDSTGLAVSN----------SDIHVVKREGELDELVETVESEiEVDGVA 68
Cdd:cd01907 1 CGIFGIMskDGEPFVGALLVEMLDAMQERGpGDGAGFALYGdpdafvyssgKDMEVFKGVGYPEDIARRYDLE-EYKGYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 69 GVGHTRWSTHGKPSDANAHPHtdCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLVGHYLDAGSSPKAAF 148
Cdd:cd01907 80 WIAHTRQPTNSAVWWYGAHPF--SIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEYY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2339760666 149 HRAV-------------------EKLEGSYAIAAvfeSRKEVMATRQDSS----LVLGVGDEATYVASDMTAL 198
Cdd:cd01907 158 KHIIrmpeeerelllalrltyrlADLDGPFTIIV---GTPDGFIVIRDRIklrpAVVAETDDYVAIASEECAI 227
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
291-410 |
6.09e-15 |
|
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: 71.88 E-value: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 291 DRVHLVACGTSYHAALFGAQMLRERGVSAQAFLASEY-AMTPAPVQDGTLVVGVTQSGETADTLAALRAADERGARTLAL 369
Cdd:cd05013 14 RRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLqLMSAANLTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAI 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2339760666 370 TNVVGSSAARECDEALYIRSGPEISVAAtkTFASQLVTLTL 410
Cdd:cd05013 94 TDSANSPLAKLADIVLLVSSEEGDFRSS--AFSSRIAQLAL 132
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
291-433 |
1.57e-14 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 74.19 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 291 DRVHLVACGTSYHAALFGAQMLRERGVSAQAF--LASEYAMTPAPVQDGTLVVGVTQSGETADTLAALRAADERGARTLA 368
Cdd:COG1737 135 RRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLdgDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIA 214
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2339760666 369 LTNVVGSSAARECDEALYIRS-GPEISVAATKTFASQ------LVTLTLFALHSSSTESNHETRRLVSALDE 433
Cdd:COG1737 215 ITDSPLSPLAKLADVVLYVPSeEPTLRSSAFSSRVAQlalidaLAAAVAQRDGDKARERLERTEALLSELRE 286
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-280 |
3.56e-12 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 69.17 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 1 MCGIIGCAGHEGDTV---PVLLNGLARLEYRGYDstglavsnsdihvvkregeldelvetvESEIEVDGVAGVGHTRWS- 76
Cdd:PRK09431 1 MCGIFGILDIKTDADelrKKALEMSRLMRHRGPD---------------------------WSGIYASDNAILGHERLSi 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 77 ---THGkpsdanAHPHTDCENRVAVVHNGIIENYQSLRDDLRSlGHEFESNTDTEVIPHLvghYLDAGsspkAAFhraVE 153
Cdd:PRK09431 54 vdvNGG------AQPLYNEDGTHVLAVNGEIYNHQELRAELGD-KYAFQTGSDCEVILAL---YQEKG----PDF---LD 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 154 KLEGSYAIAAVFESRKEVMATRqDS----SLVLGVGDEAT-YVASDMTALIERTDSVihlddGEFaflsPDGYTIIDEDG 228
Cdd:PRK09431 117 DLDGMFAFALYDSEKDAYLIAR-DPigiiPLYYGYDEHGNlYFASEMKALVPVCKTI-----KEF----PPGHYYWSKDG 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2339760666 229 ErqSKAQTTIEWdveeitkghHDHYMIKEIYEQSAALRECLRnRSTTDRLIS 280
Cdd:PRK09431 187 E--FVRYYQRDW---------FDYDAVKDNVTDKNELRDALE-AAVKKRLMS 226
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
292-400 |
1.89e-11 |
|
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: 61.44 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 292 RVHLVACGTSYHAALFGAQMLRERG-VSAQAFLASEY-AMTPAPVQDGTLVVGVTQSGETADTLAALRAADERGARTLAL 369
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESkLPVFVYNAAEFlHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90 100 110
....*....|....*....|....*....|.
gi 2339760666 370 TNVVGSSAARECDEAlyIRSGPEISVAATKT 400
Cdd:cd05710 81 TDDEDSPLAKLADYV--IVYGFEIDAVEEKY 109
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
290-540 |
6.07e-11 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 64.25 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 290 VDRVHLVACGTSYHAALfGAQMLRERGVSAQAFLASEYAM---TPAPVQDGTLVVGVTQSGETADTLAALRAADERGART 366
Cdd:PRK11382 44 IDRIYFVACGSPLNAAQ-TAKHLADRFSDLQVYAISGWEFcdnTPYRLDDRCAVIGVSDYGKTEEVIKALELGRACGALT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 367 LALTNVVGSSAARECDEALYIRSGPEISVAATKTFASQLVTLTLFALHSSSTESNHETRRLVSALdelpGQIQRLFDTT- 445
Cdd:PRK11382 123 AAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYSVVLEMITRLAPNAEIGKIKNDLKQLPNAL----GHLVRTWEEKg 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 446 -TAGEIASRLAdgsGYFFIGRGLQYPVAL-EGALKMKEITYEHAEGFAAGELKHGPLALVTDETPvFVSAVGDNETVRKT 523
Cdd:PRK11382 199 rQLGELASQWP---MIYTVAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVP-FLFLLGNDESRHTT 274
|
250
....*....|....*..
gi 2339760666 524 VANAEEVKARGAPLVAI 540
Cdd:PRK11382 275 ERAINFVKQRTDNVIVI 291
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-209 |
2.45e-10 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 63.19 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 1 MCGIIGCAGHEGDTVPVLLNGLA---RLEYRGYDStglavsnSDIHVVKREGELDELVetveseievdgvagvGHTRWST 77
Cdd:PTZ00077 1 MCGILAIFNSKGERHELRRKALElskRLRHRGPDW-------SGIIVLENSPGTYNIL---------------AHERLAI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 78 HGkPSDAnAHPHTDCENRVAVVHNGIIENYQSLRDDLRSLGHEFESNTDTEVIPHLvghYLDAGSSpkaafhRAVEKLEG 157
Cdd:PTZ00077 59 VD-LSDG-KQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHL---YKEYGPK------DFWNHLDG 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2339760666 158 SYAIAAVFESRKEVMATRQD---SSLVLGVG-DEATYVASDMTALierTDSVIHLD 209
Cdd:PTZ00077 128 MFATVIYDMKTNTFFAARDHigiIPLYIGYAkDGSIWFSSELKAL---HDQCVEVK 180
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
308-393 |
3.57e-08 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 55.10 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 308 GAQMLRERGVSAqaflaseyamtpapvqdGTLVVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEALYI 387
Cdd:COG2103 121 GAADLKALGLGP-----------------GDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIEL 183
|
....*.
gi 2339760666 388 RSGPEI 393
Cdd:COG2103 184 VTGPEV 189
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
461-542 |
4.39e-08 |
|
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: 50.84 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 461 FFIGRGLQYPVALEGALKMKEITYEHAEGFAAGELKHGPLALVTDETPV--FVSAVGDNETVRKTVANAEEvkaRGAPLV 538
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLLRKGDVviALSYSGRTEELLAALEIAKE---LGIPVI 78
|
....
gi 2339760666 539 AITD 542
Cdd:cd04795 79 AITD 82
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
340-393 |
6.35e-08 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 54.40 E-value: 6.35e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2339760666 340 VVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEALYIRSGPEI 393
Cdd:PRK05441 135 VVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEV 188
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
339-393 |
5.28e-07 |
|
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: 51.37 E-value: 5.28e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2339760666 339 LVVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEALYIRSGPEI 393
Cdd:cd05007 121 VVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEV 175
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-198 |
1.09e-06 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 51.69 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 1 MCGIIGCAGHEGDTVP--VLLNGL-ARLEYRGYDSTGLavsnsdiHVVKREGeldelvetveseievdgvagVGHTRWST 77
Cdd:PLN02549 1 MCGILAVLGCSDDSQAkrSRVLELsRRLRHRGPDWSGL-------YGNEDCY--------------------LAHERLAI 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 78 HGKPSdaNAHPHTDCENRVAVVHNGIIENYQSLRDDLRSlgHEFESNTDTEVIPHLVGHYldagsspKAAFhraVEKLEG 157
Cdd:PLN02549 54 MDPES--GDQPLYNEDKTIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHLYEEH-------GEEF---VDMLDG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2339760666 158 SYAIAAVFESRKEVMATRQD---SSLVLGVG-DEATYVASDMTAL 198
Cdd:PLN02549 120 MFSFVLLDTRDNSFIAARDHigiTPLYIGWGlDGSVWFASEMKAL 164
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
70-155 |
2.75e-06 |
|
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: 48.92 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 70 VGHTRWSTHGKPSDANAHPHTdcENRVAVVHNGIIENYQSLRDDL-RSLGHEFESNTDTEVIPHLVGHYLDAGS-SPKAA 147
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPFT--RGRWLFAHNGQLDGFRLLRRRLlRLLPRLPVGTTDSELAFALLLSRLLERDpLDPAE 161
|
....*...
gi 2339760666 148 FHRAVEKL 155
Cdd:cd01908 162 LLDAILQT 169
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
461-577 |
3.82e-06 |
|
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: 46.84 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 461 FFIGRGLQYPVALEGALKMKEItyehaeGFAAGELK--HGPLALVTDETP----VFVSAVGDNetvRKTVANAEEVKARG 534
Cdd:cd05013 17 YIFGVGSSGLVAEYLAYKLLRL------GKPVVLLSdpHLQLMSAANLTPgdvvIAISFSGET---KETVEAAEIAKERG 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2339760666 535 APLVAITD-GTSSIERLADEVLRVPSTSRELAPVLVNVQYQLLA 577
Cdd:cd05013 88 AKVIAITDsANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLA 131
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
331-370 |
1.58e-05 |
|
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: 44.56 E-value: 1.58e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2339760666 331 PAPVQDGTLVVGVTQSGETADTLAALRAADERGARTLALT 370
Cdd:cd05017 38 PAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAIT 77
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
329-385 |
2.22e-05 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 46.68 E-value: 2.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2339760666 329 MTPAPVQDGTLVVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEAL 385
Cdd:PRK11337 180 MSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
276-370 |
2.53e-05 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 46.51 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 276 DRLISLDTFDDYHSVDRVHLVACGTSYhaalFGAQMLRE---RGVSAQAFLASEYaMTPAPVQDGTLVVGVTQSGETADT 352
Cdd:PRK08674 20 EIAISLDLEEDLEKIDNIVISGMGGSG----IGGDLLRIllfDELKVPVFVNRDY-TLPAFVDEKTLVIAVSYSGNTEET 94
|
90
....*....|....*...
gi 2339760666 353 LAALRAADERGARTLALT 370
Cdd:PRK08674 95 LSAVEQALKRGAKIIAIT 112
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
401-561 |
7.01e-05 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 44.92 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 401 FASQLVTLTLFALHSSSTESNHETRRLVSALDELPGQIQRLFDTTTAGEIASRLADGSGYFFIGRGLQYPVALEGALKM- 479
Cdd:COG1737 78 LAEGLSSYERLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLl 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 480 ---KEITYEHAEGFAAGELkhgpLALVTDETPVFV-SAVGDNetvRKTVANAEEVKARGAPLVAITD-GTSSIERLADEV 554
Cdd:COG1737 158 rlgKNVVLLDGDGHLQAES----AALLGPGDVVIAiSFSGYT---RETLEAARLAKERGAKVIAITDsPLSPLAKLADVV 230
|
....*..
gi 2339760666 555 LRVPSTS 561
Cdd:COG1737 231 LYVPSEE 237
|
|
| PRK13937 |
PRK13937 |
phosphoheptose isomerase; Provisional |
335-389 |
7.21e-05 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 184408 [Multi-domain] Cd Length: 188 Bit Score: 44.08 E-value: 7.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2339760666 335 QDGTLVVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEALYIRS 389
Cdd:PRK13937 105 RPGDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLLIVPS 159
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
297-370 |
7.60e-05 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 41.59 E-value: 7.60e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2339760666 297 ACGTSYH-AALFGAQMLRERGVSAQAFLASEYAMTP--APVQDGTLVVGVTQSGETADTLAALRAADERGARTLALT 370
Cdd:cd04795 5 GIGGSGAiAAYFALELLELTGIEVVALIATELEHASllSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAIT 81
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
457-591 |
5.92e-04 |
|
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many phosphosugar isomerases and phosphosugar binding proteins. AgaS is a putative isomerase in Escherichia coli. It is similar to the glucosamine-6-phosphate synthases (GlmS) which catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source.
Pssm-ID: 240143 [Multi-domain] Cd Length: 151 Bit Score: 40.69 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339760666 457 GSGYFFigrglqyPVALEGALKMKEIT-------YEHAEGFaagelKHGPLALVTDETPVFVSAVGDNETVRKTVANAEE 529
Cdd:cd05010 5 GSGPLA-------GLAREAALKVLELTagkvatvYDSPLGF-----RHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLLKE 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2339760666 530 VKARG--APLVAITDGTSS-IERLADEVLRVPSTSRELAPVLVNVQY-QLLAYHTARHLGRKIDKP 591
Cdd:cd05010 73 LRRDGiaARVIAISPESDAgIEDNSHYYLPGSRDLDDVYLAFPYILYaQLFALFNSIALGLTPDNP 138
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
330-387 |
2.25e-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: 39.48 E-value: 2.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2339760666 330 TPApVQDGTLVVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEALYI 387
Cdd:cd05005 70 TPA-IGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVI 126
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
335-389 |
3.44e-03 |
|
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).
Pssm-ID: 240139 [Multi-domain] Cd Length: 177 Bit Score: 38.64 E-value: 3.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2339760666 335 QDGTLVVGVTQSGETADTLAALRAADERGARTLALTNVVGSSAARECDEALYIRS 389
Cdd:cd05006 100 QPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIHVPS 154
|
|
| |
